NaturalProductMech

Browse · Polyketides · kojic acid

kojic acid

CHEBI:43572 EXACT SEEDED enzyme inhibitor

What these status tags mean

Curation status describes a workflow state. SEEDED means the record entered through the source-seeding workflow; it does not imply that no later curation occurred. PROPOSED marks an addition awaiting review; REVIEWED records curator sign-off on identity, structure, filing class and producer claims; DEPRECATED retains a superseded or out-of-scope record. These are workflow decisions, not independently verified human review. Agent-assisted contributions may appear in the record history.

Grounding describes the identifier mapping: EXACT uses an ontology identity asserted by the source; MINTED keeps a local identifier when no defensible ontology identity is available; REVIEW_NEEDED flags an exact structure whose ontology identity needs adjudication. The grounding note retains any unresolved alternatives. These tags do not establish the strength of producer or activity evidence.

A pyranone that is 4H-pyran substituted by a hydroxy group at position 5, a hydroxymethyl group at position 2 and an oxo group at position 4. It has been isolated from the fungus Aspergillus oryzae.

Structure

Standard InChIKeyBEJNERDRQOWKJM-UHFFFAOYSA-N
SMILESO=C1C=C(CO)OC=C1O
Stereochemistryfully defined
Cross-referencespubchem:3840, npatlas:NPA028615

Filing pathway

Polyketides — computed by NPClassifier npclassifier.gnps2.org@2026-09-07, which is why it is pinned rather than recomputed. The gene cluster's asserted class is other, from MIBiG.

Producer organisms 1

A claim that this taxon makes the compound. The basis says what the evidence addressed — a knockout and a database assertion are not the same claim.

TaxonBasisClusterEvidence
Aspergillus oryzae RIB40
NCBITaxon:510516		 SOURCE_ASSERTION mibig:BGC0002195 DOI:10.2174/1871520618666180402141714

Occurrences 15

Somebody found the compound in this organism and cited it. That is not a claim that the organism makes it, and nothing here promotes one to the other.

TaxonSourceReference
Thalassotalea
NCBITaxon:1518149		 LOTUS DOI:10.1021/ACS.JNATPROD.5B00972
Phaeosphaeria fuckelii
NCBITaxon:178153		 LOTUS DOI:10.1021/ACS.JNATPROD.0C00046
Marrubium cylleneum
NCBITaxon:2291699		 LOTUS DOI:10.1016/J.BMC.2007.01.035
Acronychia pedunculata
NCBITaxon:354485		 LOTUS DOI:10.1021/NP030054X
Aspergillus terricola
NCBITaxon:36642		 LOTUS DOI:10.1071/CH9682775
Aspergillus candidus
NCBITaxon:41067		 LOTUS DOI:10.1080/00021369.1979.10863620
Aspergillus candidus
NCBITaxon:41067		 LOTUS DOI:10.1271/BBB1961.43.1337
Aspergillus flavus
NCBITaxon:5059		 LOTUS DOI:10.1016/J.FGB.2010.08.014
Aspergillus flavus
NCBITaxon:5059		 LOTUS DOI:10.1016/S1389-1723(01)80133-X
Aspergillus flavus
NCBITaxon:5059		 LOTUS DOI:10.1039/CT9242500575
Aspergillus flavus
NCBITaxon:5059		 LOTUS DOI:10.1080/14786419.2013.841687
Aspergillus flavus
NCBITaxon:5059		 LOTUS DOI:10.1139/M82-200
Aspergillus flavus
NCBITaxon:5059		 LOTUS DOI:10.1248/CPB.59.1174
Aspergillus oryzae
NCBITaxon:5062		 CHEBI PMID:24116376
Penicillium
NCBITaxon:5073		 LOTUS DOI:10.1021/ACS.JNATPROD.0C00741

Biosynthetic gene clusters 1

AccessionHostLocus evidenceGenome
mibig:BGC0002195 Aspergillus oryzae RIB40
NCBITaxon:510516 		CLUSTER_UNSTATED genbank:BA000053.1

A locus claim and a taxon claim are different questions. Heterologous expression settles the first and leaves the second where the isolation report left it.

Mechanism & Biosynthesis Overview

PRODUCERS & OCCURRENCE 1 producer (0 causal) 15 cited occurrences BIOSYNTHETIC LOCUS 1 gene cluster 0 curated pathway steps NATURAL PRODUCT kojic acid CHEBI:43572 Polyketides TARGETS & BIOACTIVITY 7 molecular targets 25 bioactivities · 10 graphs

Causal graph — bioactivity 3 nodes, 2 edges

Kojic acid inhibition of BindingDB-grounded Agaricus bisporus tyrosinase/polyphenol oxidase proteins.

SubjectPredicateObjectNotesEvidence
kojic acid inhibits Agaricus bisporus polyphenol oxidase 1 The source paper reported kojic acid as a 16.67 uM tyrosinase-inhibition comparator, and BindingDB/PubChem AID 1802947 maps that row to A. bisporus PPO1.
DOI:10.3109/14756366.2010.482529
  • reference
    DOI:10.3109/14756366.2010.482529
    evidence type
    PRIMARY_EXPERIMENT
kojic acid inhibits Agaricus bisporus polyphenol oxidase 2 BindingDB/PubChem AID 1799721 reports a kojic acid IC50 measurement mapped to A. bisporus PPO2.
DOI:10.1080/14756360701810207
  • reference
    DOI:10.1080/14756360701810207
    evidence type
    PRIMARY_EXPERIMENT

Every edge carries its own citation; an uncited edge is refused by the corpus tests.

Causal graph — biosynthesis 6 nodes, 5 edges

Database-qualified KojA/KojR/KojT roles in kojic-acid biosynthesis and secretion. The nodes are sequence-verified native Aspergillus oryzae RIB40 references, not verified assayed constructs or substitutes for engineered 3.042/NSPlD1 strains. KojA enzyme chemistry remains putative. No direct promoter binding, physical complex, ordered enzyme pathway or new native-production claim. The imported producer/BGC grades, computed filing class and natural-product origin remain unchanged.

SubjectPredicateObjectNotesEvidence
KojA native RIB40 reference is_database_reported_participant_in Database-reported kojic-acid biosynthesis KojA is assigned a probable enzymatic role in kojic-acid biosynthesis. The proposed glucose conversion is not an established complete reaction or a protein-alone assay. Native-reference identity and database functional attribution are separate claims; this is not a 3.042 or NSPlD1 experimental construct. No genotype-specific phenotype or physical complex is added.
https://www.uniprot.org/uniprotkb/Q2U5I0
https://www.ncbi.nlm.nih.gov/protein/BAE63185.1
https://www.ncbi.nlm.nih.gov/nuccore/BA000053.1
https://www.ncbi.nlm.nih.gov/nuccore/AP007166.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2U5I0
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed entry version 77, sequence version 1. KojA is assigned a probable enzymatic role in kojic-acid biosynthesis. The proposed glucose conversion is not an established complete reaction or a protein-alone assay. These are adopted database annotations, not newly inspected experiments. The annotations combine literature contexts, including engineered 3.042 strains; the native RIB40 reference does not establish equivalence to those assay stocks or full constructs. The cited 2010/2011 primary studies were inaccessible and the 2022 study was subscription-preview only; no experimental or disruption-phenotype edge is inferred from those citations.
    snippet
    Probable FAD-dependent monooxygenase
  • reference
    https://www.ncbi.nlm.nih.gov/protein/BAE63185.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Independent complete 428-aa RIB40 reference, taxon 510516, locus AO090113000136. Its AP007166.1 coded_by coordinates complement(1676515..1677801) and strand agree with the native CDS. Deposit identity, not independent functional or historical construct evidence.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/BA000053.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Complete CDS complement(4368691..4369977), codon_start 1/default table 1, independently translates to 428 aa identical to its annotation, GenPept BAE63185.1 and UniProt Q2U5I0. The bounded chromosome region 4368535..4374670 contains the corresponding scaffold region; this correspondence does not upgrade the imported BGC or producer evidence grade.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/AP007166.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    CDS complement(1676515..1677801) independently translates to the same complete 428-aa reference. The bounded 5776-nt scaffold region 1676515..1682290 equals its corresponding chromosome sequence. No whole-genome audit, assayed construct or 3.042 strain equality is claimed.
KojR native RIB40 reference is_database_reported_regulator_of Database-reported kojic-acid biosynthesis KojR is assigned regulation of the kojic-acid biosynthetic cluster. This does not assert direct promoter binding, protein abundance or a physical regulatory complex. Native-reference identity and database functional attribution are separate claims; this is not a 3.042 or NSPlD1 experimental construct. No genotype-specific phenotype or physical complex is added.
https://www.uniprot.org/uniprotkb/Q2U5H9
https://www.ncbi.nlm.nih.gov/protein/BAE63186.1
https://www.ncbi.nlm.nih.gov/nuccore/BA000053.1
https://www.ncbi.nlm.nih.gov/nuccore/AP007166.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2U5H9
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed entry version 101, sequence version 1. KojR is assigned regulation of the kojic-acid biosynthetic cluster. This does not assert direct promoter binding, protein abundance or a physical regulatory complex. These are adopted database annotations, not newly inspected experiments. The annotations combine literature contexts, including engineered 3.042 strains; the native RIB40 reference does not establish equivalence to those assay stocks or full constructs. The cited 2010/2011 primary studies were inaccessible and the 2022 study was subscription-preview only; no experimental or disruption-phenotype edge is inferred from those citations.
    snippet
    Transcription factor that regulates the gene cluster
  • reference
    https://www.ncbi.nlm.nih.gov/protein/BAE63186.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Independent complete 555-aa RIB40 reference, taxon 510516, locus AO090113000137. Its AP007166.1 coded_by coordinates 1678545..1680212 and strand agree with the native CDS. Deposit identity, not independent functional or historical construct evidence.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/BA000053.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Complete CDS 4370721..4372388, codon_start 1/default table 1, independently translates to 555 aa identical to its annotation, GenPept BAE63186.1 and UniProt Q2U5H9. The bounded chromosome region 4368535..4374670 contains the corresponding scaffold region; this correspondence does not upgrade the imported BGC or producer evidence grade.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/AP007166.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    CDS 1678545..1680212 independently translates to the same complete 555-aa reference. The bounded 5776-nt scaffold region 1676515..1682290 equals its corresponding chromosome sequence. No whole-genome audit, assayed construct or 3.042 strain equality is claimed.
KojT native RIB40 reference is_database_reported_participant_in Database-reported kojic-acid secretion KojT is assigned involvement in kojic-acid secretion as an MFS-type transporter. No measured transport kinetics, exclusive substrate specificity or biosynthetic enzyme activity is asserted. Native-reference identity and database functional attribution are separate claims; this is not a 3.042 or NSPlD1 experimental construct. No genotype-specific phenotype or physical complex is added.
https://www.uniprot.org/uniprotkb/Q2U5H8
https://www.ncbi.nlm.nih.gov/protein/BAE63187.1
https://www.ncbi.nlm.nih.gov/nuccore/BA000053.1
https://www.ncbi.nlm.nih.gov/nuccore/AP007166.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2U5H8
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed entry version 86, sequence version 1. KojT is assigned involvement in kojic-acid secretion as an MFS-type transporter. No measured transport kinetics, exclusive substrate specificity or biosynthetic enzyme activity is asserted. These are adopted database annotations, not newly inspected experiments. The annotations combine literature contexts, including engineered 3.042 strains; the native RIB40 reference does not establish equivalence to those assay stocks or full constructs. The cited 2010/2011 primary studies were inaccessible and the 2022 study was subscription-preview only; no experimental or disruption-phenotype edge is inferred from those citations.
    snippet
    Involved in the secretion of kojic acid
  • reference
    https://www.ncbi.nlm.nih.gov/protein/BAE63187.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Independent complete 564-aa RIB40 reference, taxon 510516, locus AO090113000138. Its AP007166.1 coded_by coordinates 1680596..1682290 and strand agree with the native CDS. Deposit identity, not independent functional or historical construct evidence.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/BA000053.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Complete CDS 4372772..4374466, codon_start 1/default table 1, independently translates to 564 aa identical to its annotation, GenPept BAE63187.1 and UniProt Q2U5H8. The bounded chromosome region 4368535..4374670 contains the corresponding scaffold region; this correspondence does not upgrade the imported BGC or producer evidence grade.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/AP007166.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    CDS 1680596..1682290 independently translates to the same complete 564-aa reference. The bounded 5776-nt scaffold region 1676515..1682290 equals its corresponding chromosome sequence. No whole-genome audit, assayed construct or 3.042 strain equality is claimed.
Database-reported kojic-acid biosynthesis has_database_reported_product kojic acid The UniProt function text names kojic acid as 5-hydroxy-2-hydroxymethyl-1,4-pyrone, matching this neutral achiral owner, CHEBI:43572/BEJNERDRQOWKJM-UHFFFAOYSA-N. No ordered pathway, specific intermediate, complete glucose-to-product reaction or protein-alone synthesis is asserted.
https://www.uniprot.org/uniprotkb/Q2U5I0
  • reference
    https://www.uniprot.org/uniprotkb/Q2U5I0
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed entry version 77, sequence version 1. KojA is assigned a probable enzymatic role in kojic-acid biosynthesis. The proposed glucose conversion is not an established complete reaction or a protein-alone assay. These are adopted database annotations, not newly inspected experiments. The annotations combine literature contexts, including engineered 3.042 strains; the native RIB40 reference does not establish equivalence to those assay stocks or full constructs. The cited 2010/2011 primary studies were inaccessible and the 2022 study was subscription-preview only; no experimental or disruption-phenotype edge is inferred from those citations.
Database-reported kojic-acid secretion has_database_reported_exported_compound kojic acid Secretion is distinct from chemical synthesis. The database names this parent kojic acid, not a derivative, salt, extract or a separately identified intracellular intermediate. No transport stoichiometry or measured protein-alone export assay is asserted.
https://www.uniprot.org/uniprotkb/Q2U5H8
  • reference
    https://www.uniprot.org/uniprotkb/Q2U5H8
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed entry version 86, sequence version 1. KojT is assigned involvement in kojic-acid secretion as an MFS-type transporter. No measured transport kinetics, exclusive substrate specificity or biosynthetic enzyme activity is asserted. These are adopted database annotations, not newly inspected experiments. The annotations combine literature contexts, including engineered 3.042 strains; the native RIB40 reference does not establish equivalence to those assay stocks or full constructs. The cited 2010/2011 primary studies were inaccessible and the 2022 study was subscription-preview only; no experimental or disruption-phenotype edge is inferred from those citations.

Every edge carries its own citation; an uncited edge is refused by the corpus tests.

Causal graph — biosynthesis 6 nodes, 5 edges

Database-qualified KpeA, AoKap1, AoKap2 and AoKap6 roles in kojic-acid production. Nodes denote sequence-verified native Aspergillus oryzae RIB40 references, not verified assayed stocks or engineered constructs. KpeA expression control remains likely; AoKap1 has a database-reported negative role; AoKap2 production regulation is distinct from its probable ferric-reductase chemistry; AoKap6 is not assigned an enzymatic reaction. No direct binding, physical complex, ordered pathway, disruption phenotype or new native-production claim is added. Existing graphs, imported producer/BGC grades, computed filing class, natural-product origin and SEEDED status remain unchanged.

SubjectPredicateObjectNotesEvidence
KpeA native RIB40 reference is_database_reported_regulator_of Database-reported kojic-acid production KpeA is assigned regulation of kojic-acid production, likely through negative control of kojR and kojA expression. The proposed expression mechanism retains the database qualifier likely; no direct promoter binding is asserted. Native-reference identity and database functional attribution remain separate claims.
https://www.uniprot.org/uniprotkb/Q2UJJ4
https://www.ncbi.nlm.nih.gov/protein/BAE58271.1
https://www.ncbi.nlm.nih.gov/nuccore/AP007155.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2UJJ4
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed entry version 74, sequence version 1. KpeA is assigned regulation of kojic-acid production, likely through negative control of kojR and kojA expression. The proposed expression mechanism retains the database qualifier likely; no direct promoter binding is asserted. Adopted database annotation, not a newly inspected functional experiment. The sequence-verified native RIB40 reference is not a verified historical assay stock, mutant or complete engineered construct. The cited primary study DOI:10.1016/j.fgb.2019.02.004 was tool-inaccessible; no alternate full text was retrieved. No disruption-phenotype, quantitative production or protein-alone synthesis claim is added.
    snippet
    kojic acid production, likely by negatively controlling kojR and kojA expression
  • reference
    https://www.ncbi.nlm.nih.gov/protein/BAE58271.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Complete native Aspergillus oryzae RIB40 reference, taxon 510516, locus AO090003001186, 762 aa. GenPept sequence and coded_by complement(join(AP007155.1:3227455..3227555,AP007155.1:3227610..3227808,AP007155.1:3227863..3228714,AP007155.1:3228779..3229915)) agree with the audited native CDS and UniProt Q2UJJ4. Deposit identity is distinct from independent functional or historical construct evidence.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/AP007155.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Complete CDS complement(join(AP007155.1:3227455..3227555,AP007155.1:3227610..3227808,AP007155.1:3227863..3228714,AP007155.1:3228779..3229915)), codon_start 1/default table 1, independently translates to 762 aa identical to the CDS annotation, GenPept BAE58271.1 and UniProt Q2UJJ4. This bounded native-reference audit does not establish chromosome/scaffold equivalence, whole-genome identity, the assayed strain or full engineered construct, or an upgraded producer/BGC evidence grade.
AoKap1 native RIB40 reference is_database_reported_negative_regulator_of Database-reported kojic-acid production AoKap1 is assigned a negative-regulatory role in kojic-acid production through effects on kojA, kojR and kojT expression. This is not direct DNA binding, protein abundance or a transport reaction. The unrelated conidiation direction is not adopted because the database and primary abstract differ on that phenotype. Native-reference identity and database functional attribution remain separate claims.
https://www.uniprot.org/uniprotkb/Q2UUI8
https://www.ncbi.nlm.nih.gov/protein/BAE54777.1
https://www.ncbi.nlm.nih.gov/nuccore/AP007150.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2UUI8
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed entry version 60, sequence version 1. AoKap1 is assigned a negative-regulatory role in kojic-acid production through effects on kojA, kojR and kojT expression. This is not direct DNA binding, protein abundance or a transport reaction. The unrelated conidiation direction is not adopted because the database and primary abstract differ on that phenotype. Adopted database annotation, not a newly inspected functional experiment. The sequence-verified native RIB40 reference is not a verified historical assay stock, mutant or complete engineered construct. The cited primary study DOI:10.1007/s00203-021-02718-4 was subscription-preview only; complete experimental methods and constructs were not inspected. No disruption-phenotype, quantitative production or protein-alone synthesis claim is added.
    snippet
    Acts as a negative regulation factor for kojic acid production
  • reference
    https://www.ncbi.nlm.nih.gov/protein/BAE54777.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Complete native Aspergillus oryzae RIB40 reference, taxon 510516, locus AO090009000298, 253 aa. GenPept sequence and coded_by complement(join(AP007150.1:794136..794520,AP007150.1:794589..794868,AP007150.1:794959..795055)) agree with the audited native CDS and UniProt Q2UUI8. Deposit identity is distinct from independent functional or historical construct evidence.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/AP007150.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Complete CDS complement(join(AP007150.1:794136..794520,AP007150.1:794589..794868,AP007150.1:794959..795055)), codon_start 1/default table 1, independently translates to 253 aa identical to the CDS annotation, GenPept BAE54777.1 and UniProt Q2UUI8. This bounded native-reference audit does not establish chromosome/scaffold equivalence, whole-genome identity, the assayed strain or full engineered construct, or an upgraded producer/BGC evidence grade.
AoKap2 native RIB40 reference is_database_reported_regulator_of Database-reported kojic-acid production AoKap2 is assigned involvement in kojic-acid production through regulation of kojA expression. No positive or negative production sign is assigned from the separate negative growth-regulation annotation. Its probable ferric-reductase chemistry is annotated by similarity and is not a demonstrated kojic-acid biosynthetic reaction. Native-reference identity and database functional attribution remain separate claims.
https://www.uniprot.org/uniprotkb/Q2U6T7
https://www.ncbi.nlm.nih.gov/protein/BAE62728.1
https://www.ncbi.nlm.nih.gov/nuccore/AP007166.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2U6T7
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed entry version 112, sequence version 1. AoKap2 is assigned involvement in kojic-acid production through regulation of kojA expression. No positive or negative production sign is assigned from the separate negative growth-regulation annotation. Its probable ferric-reductase chemistry is annotated by similarity and is not a demonstrated kojic-acid biosynthetic reaction. Adopted database annotation, not a newly inspected functional experiment. The sequence-verified native RIB40 reference is not a verified historical assay stock, mutant or complete engineered construct. The cited primary study DOI:10.1007/s11033-021-07084-4 was subscription-preview only; complete experimental methods and constructs were not inspected. No disruption-phenotype, quantitative production or protein-alone synthesis claim is added.
    snippet
    Involved in kojic acid production through the regulation of kojA expression
  • reference
    https://www.ncbi.nlm.nih.gov/protein/BAE62728.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Complete native Aspergillus oryzae RIB40 reference, taxon 510516, locus AO090120000102, 752 aa. GenPept sequence and coded_by AP007166.1:243793..246051 agree with the audited native CDS and UniProt Q2U6T7. Deposit identity is distinct from independent functional or historical construct evidence.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/AP007166.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Complete CDS AP007166.1:243793..246051, codon_start 1/default table 1, independently translates to 752 aa identical to the CDS annotation, GenPept BAE62728.1 and UniProt Q2U6T7. This bounded native-reference audit does not establish chromosome/scaffold equivalence, whole-genome identity, the assayed strain or full engineered construct, or an upgraded producer/BGC evidence grade.
AoKap6 native RIB40 reference is_database_reported_participant_in Database-reported kojic-acid production AoKap6 is assigned a role in kojic-acid synthesis with a reported upstream relationship to kojA and coordination with kojR and kojT. This does not establish an enzymatic step, direct promoter binding, a physical protein complex or an ordered biochemical pathway. Native-reference identity and database functional attribution remain separate claims.
https://www.uniprot.org/uniprotkb/Q2U5I2
https://www.ncbi.nlm.nih.gov/protein/BAE63183.1
https://www.ncbi.nlm.nih.gov/nuccore/AP007166.1
  • reference
    https://www.uniprot.org/uniprotkb/Q2U5I2
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed entry version 53, sequence version 1. AoKap6 is assigned a role in kojic-acid synthesis with a reported upstream relationship to kojA and coordination with kojR and kojT. This does not establish an enzymatic step, direct promoter binding, a physical protein complex or an ordered biochemical pathway. Adopted database annotation, not a newly inspected functional experiment. The sequence-verified native RIB40 reference is not a verified historical assay stock, mutant or complete engineered construct. The cited primary study DOI:10.1007/s11274-022-03361-x was subscription-preview only; complete experimental methods and constructs were not inspected. No disruption-phenotype, quantitative production or protein-alone synthesis claim is added.
    snippet
    Plays a role in kojic acid synthesis
  • reference
    https://www.ncbi.nlm.nih.gov/protein/BAE63183.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Complete native Aspergillus oryzae RIB40 reference, taxon 510516, locus AO090113000133, 159 aa. GenPept sequence and coded_by complement(join(AP007166.1:1670637..1670974,AP007166.1:1671090..1671231)) agree with the audited native CDS and UniProt Q2U5I2. Deposit identity is distinct from independent functional or historical construct evidence.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/AP007166.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Complete CDS complement(join(AP007166.1:1670637..1670974,AP007166.1:1671090..1671231)), codon_start 1/default table 1, independently translates to 159 aa identical to the CDS annotation, GenPept BAE63183.1 and UniProt Q2U5I2. This bounded native-reference audit does not establish chromosome/scaffold equivalence, whole-genome identity, the assayed strain or full engineered construct, or an upgraded producer/BGC evidence grade.
Database-reported kojic-acid production has_database_reported_product kojic acid The four database function annotations concern parent kojic acid, represented by this neutral achiral owner CHEBI:43572/BEJNERDRQOWKJM-UHFFFAOYSA-N. This is a production-regulation graph, not a four-enzyme pathway, a physical complex, a measured protein-alone reaction, or evidence that all four proteins were tested together.
https://www.uniprot.org/uniprotkb/Q2UJJ4
https://www.uniprot.org/uniprotkb/Q2UUI8
https://www.uniprot.org/uniprotkb/Q2U6T7
https://www.uniprot.org/uniprotkb/Q2U5I2
  • reference
    https://www.uniprot.org/uniprotkb/Q2UJJ4
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed entry version 74, sequence version 1. KpeA is assigned regulation of kojic-acid production, likely through negative control of kojR and kojA expression. The proposed expression mechanism retains the database qualifier likely; no direct promoter binding is asserted. Adopted database annotation, not a newly inspected functional experiment. The sequence-verified native RIB40 reference is not a verified historical assay stock, mutant or complete engineered construct. The cited primary study DOI:10.1016/j.fgb.2019.02.004 was tool-inaccessible; no alternate full text was retrieved. No disruption-phenotype, quantitative production or protein-alone synthesis claim is added.
  • reference
    https://www.uniprot.org/uniprotkb/Q2UUI8
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed entry version 60, sequence version 1. AoKap1 is assigned a negative-regulatory role in kojic-acid production through effects on kojA, kojR and kojT expression. This is not direct DNA binding, protein abundance or a transport reaction. The unrelated conidiation direction is not adopted because the database and primary abstract differ on that phenotype. Adopted database annotation, not a newly inspected functional experiment. The sequence-verified native RIB40 reference is not a verified historical assay stock, mutant or complete engineered construct. The cited primary study DOI:10.1007/s00203-021-02718-4 was subscription-preview only; complete experimental methods and constructs were not inspected. No disruption-phenotype, quantitative production or protein-alone synthesis claim is added.
  • reference
    https://www.uniprot.org/uniprotkb/Q2U6T7
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed entry version 112, sequence version 1. AoKap2 is assigned involvement in kojic-acid production through regulation of kojA expression. No positive or negative production sign is assigned from the separate negative growth-regulation annotation. Its probable ferric-reductase chemistry is annotated by similarity and is not a demonstrated kojic-acid biosynthetic reaction. Adopted database annotation, not a newly inspected functional experiment. The sequence-verified native RIB40 reference is not a verified historical assay stock, mutant or complete engineered construct. The cited primary study DOI:10.1007/s11033-021-07084-4 was subscription-preview only; complete experimental methods and constructs were not inspected. No disruption-phenotype, quantitative production or protein-alone synthesis claim is added.
  • reference
    https://www.uniprot.org/uniprotkb/Q2U5I2
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed entry version 53, sequence version 1. AoKap6 is assigned a role in kojic-acid synthesis with a reported upstream relationship to kojA and coordination with kojR and kojT. This does not establish an enzymatic step, direct promoter binding, a physical protein complex or an ordered biochemical pathway. Adopted database annotation, not a newly inspected functional experiment. The sequence-verified native RIB40 reference is not a verified historical assay stock, mutant or complete engineered construct. The cited primary study DOI:10.1007/s11274-022-03361-x was subscription-preview only; complete experimental methods and constructs were not inspected. No disruption-phenotype, quantitative production or protein-alone synthesis claim is added.

Every edge carries its own citation; an uncited edge is refused by the corpus tests.

Causal graph — bioactivity 2 nodes, 2 edges

Kojic-acid association with the deposited Aspergillus japonicus quercetin 2,3-dioxygenase complex 1GQH and a separate UniProt inhibition annotation. The mature protein sequence maps exactly to Q7SIC2. Structural-model existence does not independently establish inhibition, potency or a cellular effect. Ligand geometry outliers and weaker density fit for copy D remain unresolved; no primary-paper full-text or density-map validation is claimed.

SubjectPredicateObjectNotesEvidence
kojic acid has_deposited_structural_association_with A. japonicus quercetin 2,3-dioxygenase The 2.15-A X-ray model 1GQH contains four KOJ ligand copies associated with protein chains A/B/C/D. This is a qualified structural-database claim, not an independent functional assay or proof of four equivalent binding sites in solution. The model has ligand geometry outliers and copy D has weaker density fit.
https://www.rcsb.org/structure/1GQH
https://files.rcsb.org/download/1GQH.cif
https://data.rcsb.org/rest/v1/core/chemcomp/KOJ
https://files.rcsb.org/validation/view/1gqh_full_validation.pdf
  • reference
    https://www.rcsb.org/structure/1GQH
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    RCSB entry version 2.1, revised 2024-11-13, describes the kojic-acid complex at 2.15 A. The protein source is Aspergillus japonicus (taxon 34381); Aspergillus awamori (taxon 105351) is the expression host, not the protein source or a newly established kojic-acid producer. The asymmetric unit has four protein chains; two author/PISA dimer assemblies are not a solution tetramer claim. Primary DOI:10.1021/bi0159736 was tool-inaccessible; its embedded abstract does not count as inspected full text, figures or supplements.
    snippet
    Quercetin 2,3-dioxygenase in complex with the inhibitor kojic acid
  • reference
    https://files.rcsb.org/download/1GQH.cif
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Independent comparison of the deposited 350-aa mature sequence and all polymer positions gives exact identity to reviewed UniProt Q7SIC2 version 81, sequence version 1. The CIF struct_ref points to PDB rather than UniProt; mapping is by sequence, not that field. Modeled residues A/B/C/D are 341/334/333/331, leaving 9/16/17/19 unmodeled. Four KOJ copies at author residue 1351 use label chains I/O/T/Y, with ten heavy atoms, occupancy 1 and no alternates per copy. These are deposited-model values, not validated affinities or occupancies in solution. No native CDS, complete tagged expression construct or historical assay-stock equivalence is established. Metal-contact distances were not independently computed.
  • reference
    https://data.rcsb.org/rest/v1/core/chemcomp/KOJ
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The CCD KOJ definition has neutral achiral formula C6H6O4 and Standard InChI and InChIKey identical to this owner, CHEBI:43572/BEJNERDRQOWKJM-UHFFFAOYSA-N. That chemical-component identity is not proof of the ligand protonation state in the metal complex; no salt, derivative or different inhibitor is substituted.
  • reference
    https://files.rcsb.org/validation/view/1gqh_full_validation.pdf
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Text of the 40-page wwPDB report dated 2026-03-06 was inspected. All four KOJ copies have bond-length/angle outliers; A/B also have torsion outliers. Reported RSCC/RSR for A/B/C/D are 0.89/0.10, 0.91/0.12, 0.81/0.12 and 0.69/0.23, respectively; copy D has weaker density fit. All copies model 10/10 heavy atoms with none at occupancy below 0.9. Glycan MAN chirality concerns also remain. No refinement or independent density-map interpretation was performed. Screenshot attempts produced no inspectable images and the last attempt timed out; no pixel inspection or alternate report retrieval is claimed.
kojic acid is_database_reported_inhibitor_of A. japonicus quercetin 2,3-dioxygenase UniProt reports inhibition of this A. japonicus enzyme by kojic acid. This adopted database annotation is separate from the deposited structural association. No Ki, IC50, inhibition mode, direct binding measurement, downstream cellular effect or antimicrobial phenotype is added.
https://www.uniprot.org/uniprotkb/Q7SIC2
  • reference
    https://www.uniprot.org/uniprotkb/Q7SIC2
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed entry version 81, sequence version 1, 350 aa, Aspergillus japonicus taxon 34381. Its activity-regulation annotation names kojic acid as an inhibitor. Its PDB cross-reference specifically lists 1GQH at 2.15 A; 1GQG is the different diethyldithiocarbamate complex at 1.70 A and is not substituted. The deposited mature sequence was independently matched to Q7SIC2, not to a convenient homolog. This does not establish the native gene or complete assay construct. Cited primary DOI:10.1021/bi0159736 remained tool-inaccessible, so no new primary experimental or quantitative claim is made.
    snippet
    Inhibited by diethyldithiocarbamate and kojic acid

Every edge carries its own citation; an uncited edge is refused by the corpus tests.

Causal graph — biosynthesis 6 nodes, 5 edges

Database-qualified A. flavus KojA/KojR/KojT roles in kojic-acid biosynthesis, regulation and probable secretion. Nodes denote sequence-verified native NRRL3357 references, not verified historical stocks or engineered constructs. KojA chemistry and KojT secretion remain probable; cluster regulation is not an independently verified promoter-binding site. Native-reference evidence retains species-level versus strain-level deposit taxonomy. No ordered enzyme pathway, physical complex, disruption phenotype, quantitative production or producer/BGC-grade upgrade is asserted. The existing A. oryzae graphs and imported RIB40 BGC are separate, unchanged claims.

SubjectPredicateObjectNotesEvidence
KojA native A. flavus NRRL3357 reference is_database_reported_probable_participant_in Database-reported kojic-acid biosynthesis KojA is annotated as a probable FAD-dependent monooxygenase involved in kojic-acid biosynthesis. Possible glucose conversion and participation of additional enzymes remain by-similarity proposals, not an established complete reaction or a protein-alone assay. Native-reference identity and database functional attribution remain separate claims.
https://www.uniprot.org/uniprotkb/B8NL20
https://www.ncbi.nlm.nih.gov/protein/EED49522.1
https://www.ncbi.nlm.nih.gov/nuccore/EQ963480.1
https://www.ncbi.nlm.nih.gov/protein/QRD85033.1
https://www.ncbi.nlm.nih.gov/nuccore/CP044621.1
https://www.ncbi.nlm.nih.gov/protein/QMW33428.1
https://www.ncbi.nlm.nih.gov/nuccore/CP059870.1
  • reference
    https://www.uniprot.org/uniprotkb/B8NL20
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed entry version 63, sequence version 1. KojA is annotated as a probable FAD-dependent monooxygenase involved in kojic-acid biosynthesis. Possible glucose conversion and participation of additional enzymes remain by-similarity proposals, not an established complete reaction or a protein-alone assay. Adopted database annotation, not a newly inspected functional experiment. The native NRRL3357 reference is not a verified historical assay stock, mutant or complete engineered construct. Cited primary DOI:10.3390/jof9020259 was tool-inaccessible; no alternate full text was retrieved. No disruption-phenotype, quantitative production or producer/BGC-grade upgrade is added.
    snippet
    Probable FAD-dependent monooxygenase
  • reference
    https://www.ncbi.nlm.nih.gov/protein/EED49522.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Complete native Aspergillus flavus NRRL3357 reference, locus AFLA_096040, 428 aa. GenPept sequence and coded_by complement(EQ963480.1:1860021..1861307) agree with the independently audited CDS and UniProt B8NL20. The deposit uses strain taxon 332952, matching the UniProt reference. Reference identity does not establish an assayed stock, full construct or experimental function.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/EQ963480.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Complete CDS complement(EQ963480.1:1860021..1861307), codon_start 1/default table 1, independently translates to 428 aa identical to its annotation, GenPept EED49522.1 and UniProt B8NL20. The deposit uses strain taxon 332952, matching the UniProt reference. The bounded EQ963480.1:1860021..1865796 and CP044621.1:4359976..4365751 regions are nucleotide-identical (5776 nt). Bounded correspondence is not whole-genome, historical-stock or full assay-construct equality; it does not transfer the RIB40 BGC or producer claim to A. flavus.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/QRD85033.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Complete native Aspergillus flavus NRRL3357 reference, locus F9C07_9288, 428 aa. GenPept sequence and coded_by complement(CP044621.1:4359976..4361262) agree with the independently audited CDS and UniProt B8NL20. The deposit uses species-level taxon 5059 with explicit strain NRRL 3357; it is not relabelled as strain taxon 332952. Reference identity does not establish an assayed stock, full construct or experimental function.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/CP044621.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Complete CDS complement(CP044621.1:4359976..4361262), codon_start 1/default table 1, independently translates to 428 aa identical to its annotation, GenPept QRD85033.1 and UniProt B8NL20. The deposit uses species-level taxon 5059 with explicit strain NRRL 3357; it is not relabelled as strain taxon 332952. The bounded EQ963480.1:1860021..1865796 and CP044621.1:4359976..4365751 regions are nucleotide-identical (5776 nt). Bounded correspondence is not whole-genome, historical-stock or full assay-construct equality; it does not transfer the RIB40 BGC or producer claim to A. flavus.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/QMW33428.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Complete native Aspergillus flavus NRRL3357 reference, locus G4B84_008859, 428 aa. GenPept sequence and coded_by complement(CP059870.1:4265240..4266526) agree with the independently audited CDS and UniProt B8NL20. The deposit uses strain taxon 332952, matching the UniProt reference. Reference identity does not establish an assayed stock, full construct or experimental function.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/CP059870.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Complete CDS complement(CP059870.1:4265240..4266526), codon_start 1/default table 1, independently translates to 428 aa identical to its annotation, GenPept QMW33428.1 and UniProt B8NL20. The deposit uses strain taxon 332952, matching the UniProt reference. The bounded CP059870.1:4265240..4268937 region equals the first 3698 nt of the audited scaffold/chromosome intervals. This slice covers KojA/R only; it does not establish absence of KojT from the assembly. Bounded correspondence is not whole-genome, historical-stock or full assay-construct equality; it does not transfer the RIB40 BGC or producer claim to A. flavus.
KojR native A. flavus NRRL3357 reference is_database_reported_regulator_of Database-reported kojic-acid biosynthesis KojR is annotated as regulating the kojic-acid gene cluster, including kojA and kojT expression. This graph adopts cluster regulation; it does not independently verify a promoter-binding site, genotype-specific phenotype or physical regulatory complex. Native-reference identity and database functional attribution remain separate claims.
https://www.uniprot.org/uniprotkb/B8NL21
https://www.ncbi.nlm.nih.gov/protein/EED49523.1
https://www.ncbi.nlm.nih.gov/nuccore/EQ963480.1
https://www.ncbi.nlm.nih.gov/protein/QRD85034.1
https://www.ncbi.nlm.nih.gov/nuccore/CP044621.1
https://www.ncbi.nlm.nih.gov/protein/QMW33429.1
https://www.ncbi.nlm.nih.gov/nuccore/CP059870.1
  • reference
    https://www.uniprot.org/uniprotkb/B8NL21
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed entry version 96, sequence version 1. KojR is annotated as regulating the kojic-acid gene cluster, including kojA and kojT expression. This graph adopts cluster regulation; it does not independently verify a promoter-binding site, genotype-specific phenotype or physical regulatory complex. Adopted database annotation, not a newly inspected functional experiment. The native NRRL3357 reference is not a verified historical assay stock, mutant or complete engineered construct. Cited primary DOI:10.3390/jof9020259 was tool-inaccessible; no alternate full text was retrieved. No disruption-phenotype, quantitative production or producer/BGC-grade upgrade is added.
    snippet
    Transcription factor that regulates the gene cluster
  • reference
    https://www.ncbi.nlm.nih.gov/protein/EED49523.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Complete native Aspergillus flavus NRRL3357 reference, locus AFLA_096050, 555 aa. GenPept sequence and coded_by EQ963480.1:1862051..1863718 agree with the independently audited CDS and UniProt B8NL21. The deposit uses strain taxon 332952, matching the UniProt reference. Reference identity does not establish an assayed stock, full construct or experimental function.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/EQ963480.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Complete CDS EQ963480.1:1862051..1863718, codon_start 1/default table 1, independently translates to 555 aa identical to its annotation, GenPept EED49523.1 and UniProt B8NL21. The deposit uses strain taxon 332952, matching the UniProt reference. The bounded EQ963480.1:1860021..1865796 and CP044621.1:4359976..4365751 regions are nucleotide-identical (5776 nt). Bounded correspondence is not whole-genome, historical-stock or full assay-construct equality; it does not transfer the RIB40 BGC or producer claim to A. flavus.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/QRD85034.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Complete native Aspergillus flavus NRRL3357 reference, locus F9C07_9289, 555 aa. GenPept sequence and coded_by CP044621.1:4362006..4363673 agree with the independently audited CDS and UniProt B8NL21. The deposit uses species-level taxon 5059 with explicit strain NRRL 3357; it is not relabelled as strain taxon 332952. Reference identity does not establish an assayed stock, full construct or experimental function.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/CP044621.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Complete CDS CP044621.1:4362006..4363673, codon_start 1/default table 1, independently translates to 555 aa identical to its annotation, GenPept QRD85034.1 and UniProt B8NL21. The deposit uses species-level taxon 5059 with explicit strain NRRL 3357; it is not relabelled as strain taxon 332952. The bounded EQ963480.1:1860021..1865796 and CP044621.1:4359976..4365751 regions are nucleotide-identical (5776 nt). Bounded correspondence is not whole-genome, historical-stock or full assay-construct equality; it does not transfer the RIB40 BGC or producer claim to A. flavus.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/QMW33429.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Complete native Aspergillus flavus NRRL3357 reference, locus G4B84_008860, 555 aa. GenPept sequence and coded_by CP059870.1:4267270..4268937 agree with the independently audited CDS and UniProt B8NL21. The deposit uses strain taxon 332952, matching the UniProt reference. Reference identity does not establish an assayed stock, full construct or experimental function.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/CP059870.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Complete CDS CP059870.1:4267270..4268937, codon_start 1/default table 1, independently translates to 555 aa identical to its annotation, GenPept QMW33429.1 and UniProt B8NL21. The deposit uses strain taxon 332952, matching the UniProt reference. The bounded CP059870.1:4265240..4268937 region equals the first 3698 nt of the audited scaffold/chromosome intervals. This slice covers KojA/R only; it does not establish absence of KojT from the assembly. Bounded correspondence is not whole-genome, historical-stock or full assay-construct equality; it does not transfer the RIB40 BGC or producer claim to A. flavus.
KojT native A. flavus NRRL3357 reference is_database_reported_probable_participant_in Database-proposed kojic-acid secretion KojT is annotated as an MFS-type transporter with a probable role in kojic-acid secretion. Secretion is not chemical synthesis. No measured transport kinetics, exclusive substrate specificity or experimentally established protein-alone transport is asserted. Native-reference identity and database functional attribution remain separate claims.
https://www.uniprot.org/uniprotkb/B8NL22
https://www.ncbi.nlm.nih.gov/protein/EED49524.1
https://www.ncbi.nlm.nih.gov/nuccore/EQ963480.1
https://www.ncbi.nlm.nih.gov/protein/QRD85035.1
https://www.ncbi.nlm.nih.gov/nuccore/CP044621.1
  • reference
    https://www.uniprot.org/uniprotkb/B8NL22
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed entry version 68, sequence version 1. KojT is annotated as an MFS-type transporter with a probable role in kojic-acid secretion. Secretion is not chemical synthesis. No measured transport kinetics, exclusive substrate specificity or experimentally established protein-alone transport is asserted. Adopted database annotation, not a newly inspected functional experiment. The native NRRL3357 reference is not a verified historical assay stock, mutant or complete engineered construct. Cited primary DOI:10.3390/jof9020259 was tool-inaccessible; no alternate full text was retrieved. No disruption-phenotype, quantitative production or producer/BGC-grade upgrade is added.
    snippet
    Involved in the secretion of kojic acid (Probable)
  • reference
    https://www.ncbi.nlm.nih.gov/protein/EED49524.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Complete native Aspergillus flavus NRRL3357 reference, locus AFLA_096060, 564 aa. GenPept sequence and coded_by EQ963480.1:1864102..1865796 agree with the independently audited CDS and UniProt B8NL22. The deposit uses strain taxon 332952, matching the UniProt reference. Reference identity does not establish an assayed stock, full construct or experimental function.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/EQ963480.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Complete CDS EQ963480.1:1864102..1865796, codon_start 1/default table 1, independently translates to 564 aa identical to its annotation, GenPept EED49524.1 and UniProt B8NL22. The deposit uses strain taxon 332952, matching the UniProt reference. The bounded EQ963480.1:1860021..1865796 and CP044621.1:4359976..4365751 regions are nucleotide-identical (5776 nt). Bounded correspondence is not whole-genome, historical-stock or full assay-construct equality; it does not transfer the RIB40 BGC or producer claim to A. flavus.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/QRD85035.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Complete native Aspergillus flavus NRRL3357 reference, locus F9C07_9290, 564 aa. GenPept sequence and coded_by CP044621.1:4364057..4365751 agree with the independently audited CDS and UniProt B8NL22. The deposit uses species-level taxon 5059 with explicit strain NRRL 3357; it is not relabelled as strain taxon 332952. Reference identity does not establish an assayed stock, full construct or experimental function.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/CP044621.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Complete CDS CP044621.1:4364057..4365751, codon_start 1/default table 1, independently translates to 564 aa identical to its annotation, GenPept QRD85035.1 and UniProt B8NL22. The deposit uses species-level taxon 5059 with explicit strain NRRL 3357; it is not relabelled as strain taxon 332952. The bounded EQ963480.1:1860021..1865796 and CP044621.1:4359976..4365751 regions are nucleotide-identical (5776 nt). Bounded correspondence is not whole-genome, historical-stock or full assay-construct equality; it does not transfer the RIB40 BGC or producer claim to A. flavus.
Database-reported kojic-acid biosynthesis has_database_reported_product kojic acid The source function text names 5-hydroxy-2-hydroxymethyl-1,4-pyrone, matching this neutral achiral kojic-acid owner CHEBI:43572/BEJNERDRQOWKJM-UHFFFAOYSA-N. No ordered pathway, specific intermediate, complete glucose-to-product reaction or protein-alone synthesis is asserted.
https://www.uniprot.org/uniprotkb/B8NL20
  • reference
    https://www.uniprot.org/uniprotkb/B8NL20
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed entry version 63, sequence version 1. KojA is annotated as a probable FAD-dependent monooxygenase involved in kojic-acid biosynthesis. Possible glucose conversion and participation of additional enzymes remain by-similarity proposals, not an established complete reaction or a protein-alone assay. Adopted database annotation, not a newly inspected functional experiment. The native NRRL3357 reference is not a verified historical assay stock, mutant or complete engineered construct. Cited primary DOI:10.3390/jof9020259 was tool-inaccessible; no alternate full text was retrieved. No disruption-phenotype, quantitative production or producer/BGC-grade upgrade is added.
Database-proposed kojic-acid secretion has_database_proposed_exported_compound kojic acid The probable secretion annotation concerns parent kojic acid, not a derivative, salt, extract or separately identified intermediate. No measured transport stoichiometry or protein-alone export assay is asserted.
https://www.uniprot.org/uniprotkb/B8NL22
  • reference
    https://www.uniprot.org/uniprotkb/B8NL22
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed entry version 68, sequence version 1. KojT is annotated as an MFS-type transporter with a probable role in kojic-acid secretion. Secretion is not chemical synthesis. No measured transport kinetics, exclusive substrate specificity or experimentally established protein-alone transport is asserted. Adopted database annotation, not a newly inspected functional experiment. The native NRRL3357 reference is not a verified historical assay stock, mutant or complete engineered construct. Cited primary DOI:10.3390/jof9020259 was tool-inaccessible; no alternate full text was retrieved. No disruption-phenotype, quantitative production or producer/BGC-grade upgrade is added.

Every edge carries its own citation; an uncited edge is refused by the corpus tests.

Causal graph — bioactivity 3 nodes, 2 edges

Database-qualified kojic-acid inhibition of in-vitro quercetinase activity annotated for human PIR and E. coli YhhW. These are two separate protein references, not a cross-species complex or an assertion that they were assayed together. Four native CDS translations ground reference identity, not historical assay stocks or full expression constructs. No direct binding, inhibition constant or mode, physiological function, NF-kappa-B response, cellular phenotype, antimicrobial activity or new producer/BGC claim is inferred.

SubjectPredicateObjectNotesEvidence
kojic acid is_database_reported_inhibitor_of Human pirin (PIR) UniProt reports inhibition by parent kojic acid of the annotated in-vitro quercetinase activity. The compound is the neutral achiral owner CHEBI:43572, not an extract, derivative or other inhibitor listed alongside it. No measured Ki/IC50, direct binding, chelation mechanism or downstream cellular effect is added.
https://www.uniprot.org/uniprotkb/O00625
https://www.ncbi.nlm.nih.gov/protein/CAA69195.1
https://www.ncbi.nlm.nih.gov/nuccore/Y07868.1
https://www.ncbi.nlm.nih.gov/protein/CAA69194.1
https://www.ncbi.nlm.nih.gov/nuccore/Y07867.1
  • reference
    https://www.uniprot.org/uniprotkb/O00625
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed PIR entry version 193, sequence version 1, Homo sapiens taxon 9606, 290 aa. Function is annotated as in-vitro quercetin 2,3-dioxygenase activity; activity regulation names kojic acid and cites PMID:15951572/DOI:10.1074/jbc.m501034200. The primary paper was tool-inaccessible and no alternate text, figures or supplements were retrieved. This is an adopted database annotation, not an independently inspected functional assay. CAG46621 conflicts V24D/K162R and natural variant V228A are not substituted for the canonical reference. PIR transcriptional/NF-kappa-B roles do not establish a kojic-acid cellular mechanism.
    snippet
    Inhibited by kojic acid
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CAA69195.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Independent complete 290-aa human reference, taxon 9606, HeLa-derived pDR-Pirin #17, lambda DR2 library. GenPept and coded_by Y07868.1:231..1103 agree with the audited CDS and UniProt O00625. The deposited clone is not a verified 2005 assay stock or full tagged construct.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/Y07868.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete CDS 231..1103 in the 1318-nt mRNA, codon_start 1/default translation table 1, independently translates to 290 aa identical to the annotation, GenPept CAA69195.1 and UniProt O00625. HeLa clone/library metadata establishes native-reference provenance, not a kojic-acid cell assay, historical preparation or functional measurement.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/CAA69194.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Independent complete 290-aa human reference, taxon 9606, HeLa-derived pDR-Pirin #1, lambda DR2 library. GenPept and coded_by Y07867.1:205..1077 agree with the audited CDS and UniProt O00625. The deposited clone is not a verified 2005 assay stock or full tagged construct.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/Y07867.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete CDS 205..1077 in the 1292-nt mRNA, codon_start 1/default translation table 1, independently translates to 290 aa identical to the annotation, GenPept CAA69194.1 and UniProt O00625. HeLa clone/library metadata establishes native-reference provenance, not a kojic-acid cell assay, historical preparation or functional measurement.
kojic acid is_database_reported_inhibitor_of E. coli K12 quercetinase YhhW UniProt reports inhibition by parent kojic acid of the annotated in-vitro quercetinase activity. The compound is the neutral achiral owner CHEBI:43572, not an extract, derivative or other inhibitor listed alongside it. No measured Ki/IC50, direct binding, chelation mechanism or downstream cellular effect is added.
https://www.uniprot.org/uniprotkb/P46852
https://www.ncbi.nlm.nih.gov/protein/AAC76464.1
https://www.ncbi.nlm.nih.gov/nuccore/U00096.3
https://www.ncbi.nlm.nih.gov/protein/BAE77854.1
https://www.ncbi.nlm.nih.gov/nuccore/AP009048.1
  • reference
    https://www.uniprot.org/uniprotkb/P46852
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed YhhW entry version 158, sequence version 1, 231 aa, Escherichia coli K12 taxon 83333. In-vitro quercetinase activity and kojic-acid inhibition are annotated with PMID:15951572/DOI:10.1074/jbc.m501034200. The primary paper remained tool-inaccessible; no alternate full text, figures or supplements were retrieved. Its tentative physiological quercetin-protection hypothesis is not a demonstrated kojic-acid mechanism or an antimicrobial-resistance phenotype. The cited 1TQ5 cadmium structure is not adopted as a kojic-acid complex; no structural binding claim is made.
    snippet
    Inhibited by kojic acid
  • reference
    https://www.ncbi.nlm.nih.gov/protein/AAC76464.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Independent complete 231-aa E. coli K-12 MG1655 reference, taxon 511145, yhhW/b3439. GenPept and coded_by complement(U00096.3:3578950..3579645) agree with the audited CDS and UniProt P46852. The deposit retains its substrain taxonomy; it is not relabeled as the generic K12 taxon or identified as the historical assay stock.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/U00096.3
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete CDS complement(3578950..3579645), read from its bounded 696-nt genome interval, codon_start 1/table 11, independently translates to 231 aa identical to its annotation, GenPept AAC76464.1 and UniProt P46852. Protein-sequence correspondence does not establish nucleotide identity between MG1655 and W3110, whole-genome equivalence, the 2005 assay substrain or a complete engineered expression construct.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/BAE77854.1
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Independent complete 231-aa E. coli K-12 W3110 reference, taxon 316407, yhhW. GenPept and coded_by AP009048.1:4060770..4061465 agree with the audited CDS and UniProt P46852. The deposit retains its substrain taxonomy; it is not relabeled as the generic K12 taxon or identified as the historical assay stock.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/AP009048.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete CDS 4060770..4061465, read from its bounded 696-nt genome interval, codon_start 1/table 11, independently translates to 231 aa identical to its annotation, GenPept BAE77854.1 and UniProt P46852. Protein-sequence correspondence does not establish nucleotide identity between MG1655 and W3110, whole-genome equivalence, the 2005 assay substrain or a complete engineered expression construct.

Every edge carries its own citation; an uncited edge is refused by the corpus tests.

Causal graph — bioactivity 2 nodes, 1 edge

Database-qualified inhibition of apricot PPO by parent kojic acid. Native reference precursor identity and database processing annotations are retained separately from the unverified assay preparation. This is not a direct binding assay, inhibition constant, chelation mechanism, human pigmentation effect, antimicrobial phenotype or claim that apricot produces kojic acid.

SubjectPredicateObjectNotesEvidence
kojic acid is_database_reported_inhibitor_of Apricot polyphenol oxidase (PPO; reference precursor) The accession denotes the 597-aa reference precursor, not a claim that the intact precursor was the assayed species. UniProt annotates latent 102..597 and active 102..429 chains and cleavage at 429..430; processing and historical assay preparation were not independently verified. Substrate Km values are not kojic-acid Ki or IC50 values.
https://www.uniprot.org/uniprotkb/O81103
https://www.ncbi.nlm.nih.gov/protein/AAC28935.1
https://www.ncbi.nlm.nih.gov/nuccore/AF020786.1
  • reference
    https://www.uniprot.org/uniprotkb/O81103
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed entry version 96, sequence version 1, Prunus armeniaca taxon 36596. Activity regulation names kojic acid; the annotation cites PMID:10198084 and PMID:28812349. DOI:10.1021/acs.jafc.7b03210 returned HTTP 403 and DOI:10.1104/pp.119.4.1261 was tool-inaccessible; no alternate retrieval. This adopts a database annotation, not an independently inspected experiment. No monophenol oxidation is inferred from a generic function description.
    snippet
    Repressed by several inhibitors including 4-hexylresorcinol, ascorbic acid, benzoic acid, kojic acid
  • reference
    https://www.ncbi.nlm.nih.gov/protein/AAC28935.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Independent curator sequence/model comparison using the deposited reference; quoted titles and source metadata remain attributed to the deposit. Complete 597-aa native reference agrees exactly with UniProt O81103. Deposited Prunus armeniaca Bergeron, clone pAPRI101G, mesocarp/exocarp of green fruit. This does not establish the 2017 assay cultivar, stock, peptides or full construct.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/AF020786.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The 2070-nt mRNA CDS 4..1797, codon_start 1/default table 1, independently translates to 597 aa identical to the CDS annotation, AAC28935.1 and O81103. Native CDS correspondence establishes reference identity, not processing or inhibition.

Every edge carries its own citation; an uncited edge is refused by the corpus tests.

Causal graph — bioactivity 3 nodes, 2 edges

Deposited kojic-acid associations with two distinct engineered fragments of human TYRP1, not human tyrosinase TYR. Canonical P17643 grounds reference identity while node labels and evidence retain truncation and mutation differences. DOI:10.1002/anie.201704616 was tool-inaccessible; no alternate retrieval or primary functional experiment is adopted. Structural association is not a direct binding assay, measured inhibition, affinity or inhibition mode, physiological metal stoichiometry, cellular phenotype, or a producer/BGC claim. Protein engineering here does not change the natural-product origin classification.

SubjectPredicateObjectNotesEvidence
kojic acid has_deposited_structural_association_with Human TYRP1 25..470 (5M8M; wild-type sequence) Construct-specific association in PDB:5M8M; canonical UniProt grounds the reference protein, not an assertion that this is the intact native protein. The deposited title is quoted as metadata, not independently verified inhibition or active-site chemistry. Ligand geometry and density-fit limitations are retained in the validation evidence.
https://www.rcsb.org/structure/5M8M
https://www.uniprot.org/uniprotkb/P17643
https://www.ncbi.nlm.nih.gov/protein/AAH52608.1
https://www.ncbi.nlm.nih.gov/nuccore/BC052608.1
https://data.rcsb.org/rest/v1/core/chemcomp/KOJ
https://files.rcsb.org/validation/view/5m8m_full_validation.pdf
  • reference
    https://www.rcsb.org/structure/5M8M
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Independent curator sequence/model comparison using the deposited reference; quoted titles and source metadata remain attributed to the deposit. PDB revision 3.0, X-ray resolution 2.65 angstrom. Deposited 446-aa wild-type-sequence fragment of human TYRP1 positions 25..470; each modeled polymer residue in chains A/B/C/D matches that construct, including all 446 residue positions, not necessarily every side-chain atom. Native source is Homo sapiens taxon 9606; expression host Spodoptera frugiperda taxon 7108, cell line/vector unspecified. KOJ copies at author A503/B504/C503/D504 (label chains AA/EA/HA/LA), each ten heavy atoms at modeled occupancy 1 without alternates. Nine deposited Zn ions are an inventory, not physiological stoichiometry. Four deposited monomeric assemblies do not establish a tetramer.
    snippet
    Crystal structure of human tyrosinase related protein 1 in complex with kojic acid
  • reference
    https://www.uniprot.org/uniprotkb/P17643
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed TYRP1 entry version 224, sequence version 2, Homo sapiens taxon 9606, 537-aa precursor. TYRP1 is not TYR/P14679. UniProt cautions that DHICA oxidase activity is controversial and metal-dependent, absent with Zn in the cited annotation. No kojic-acid inhibition annotation is adopted. The graph uses PROTEIN, not a claim of active Zn-loaded enzyme.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/AAH52608.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Independent curator sequence/model comparison using the deposited reference; quoted titles and source metadata remain attributed to the deposit. Complete 537-aa human reference; clone MGC:59834 IMAGE:6258285, skin melanoma/melanotic tissue. Sequence agrees with P17643, unlike older conflicting references. DH10B-R/pOTB7 is cloning metadata, not the crystallographic expression host or a kojic-acid cellular assay.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/BC052608.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The 2628-nt mRNA CDS 98..1711, codon_start 1/default table 1, independently translates to 537 aa identical to AAH52608.1 and P17643. Fragment boundaries and any substitutions are separately resolved against this reference; no full expression plasmid or historical assay-stock identity is established.
  • reference
    https://data.rcsb.org/rest/v1/core/chemcomp/KOJ
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    CCD KOJ has neutral charge, C6H6O4, no chiral atoms and the same StandardInChI and InChIKey as CHEBI:43572. This establishes deposited component identity, not protonation or coordination in the metal complex.
  • reference
    https://files.rcsb.org/validation/view/5m8m_full_validation.pdf
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Report dated 2026-03-05, inspected ligand sections on pages 48-50 and 70. All four KOJ copies have bond-length and bond-angle outliers; A/D torsion outliers; D has one short contact. KOJ A503/B504/C503/D504 RSCC/RSR are 0.93/0.10, 0.88/0.13, 0.89/0.13, 0.85/0.14. Reported ligand geometry/density-fit caveats remain unresolved; no independent map interpretation, distance/contact calculation, protonation, refinement, full side-chain or whole-model quality audit was performed.
kojic acid has_deposited_structural_association_with Human TYRP1 25..470 Y362F/R374S/T391V (5M8Q) Construct-specific association in PDB:5M8Q; canonical UniProt grounds the reference protein, not an assertion that this is the intact native protein. The deposited title is quoted as metadata, not independently verified inhibition or active-site chemistry. Ligand geometry and density-fit limitations are retained in the validation evidence.
https://www.rcsb.org/structure/5M8Q
https://www.uniprot.org/uniprotkb/P17643
https://www.ncbi.nlm.nih.gov/protein/AAH52608.1
https://www.ncbi.nlm.nih.gov/nuccore/BC052608.1
https://data.rcsb.org/rest/v1/core/chemcomp/KOJ
https://files.rcsb.org/validation/view/5m8q_full_validation.pdf
  • reference
    https://www.rcsb.org/structure/5M8Q
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Independent curator sequence/model comparison using the deposited reference; quoted titles and source metadata remain attributed to the deposit. PDB revision 2.1, X-ray resolution 2.85 angstrom. Deposited 446-aa fragment of human TYRP1 positions 25..470 with Y362F/R374S/T391V substitutions; each modeled polymer residue in chains A/B/C/D matches that construct, including all 446 residue positions, not necessarily every side-chain atom. Native source is Homo sapiens taxon 9606; expression host Spodoptera frugiperda taxon 7108, cell line/vector unspecified. KOJ copies at author A516/B508/C514/D510 (label chains S/Y/DA/IA), each ten heavy atoms at modeled occupancy 1 without alternates. Nine deposited Zn ions are an inventory, not physiological stoichiometry. Four deposited monomeric assemblies do not establish a tetramer.
    snippet
    Crystal structure of human tyrosinase related protein 1 mutant (T391V-R374S-Y362F) in complex with kojic acid
  • reference
    https://www.uniprot.org/uniprotkb/P17643
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Reviewed TYRP1 entry version 224, sequence version 2, Homo sapiens taxon 9606, 537-aa precursor. TYRP1 is not TYR/P14679. UniProt cautions that DHICA oxidase activity is controversial and metal-dependent, absent with Zn in the cited annotation. No kojic-acid inhibition annotation is adopted. The graph uses PROTEIN, not a claim of active Zn-loaded enzyme.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/AAH52608.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Independent curator sequence/model comparison using the deposited reference; quoted titles and source metadata remain attributed to the deposit. Complete 537-aa human reference; clone MGC:59834 IMAGE:6258285, skin melanoma/melanotic tissue. Sequence agrees with P17643, unlike older conflicting references. DH10B-R/pOTB7 is cloning metadata, not the crystallographic expression host or a kojic-acid cellular assay.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/BC052608.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The 2628-nt mRNA CDS 98..1711, codon_start 1/default table 1, independently translates to 537 aa identical to AAH52608.1 and P17643. Fragment boundaries and any substitutions are separately resolved against this reference; no full expression plasmid or historical assay-stock identity is established.
  • reference
    https://data.rcsb.org/rest/v1/core/chemcomp/KOJ
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    CCD KOJ has neutral charge, C6H6O4, no chiral atoms and the same StandardInChI and InChIKey as CHEBI:43572. This establishes deposited component identity, not protonation or coordination in the metal complex.
  • reference
    https://files.rcsb.org/validation/view/5m8q_full_validation.pdf
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Report dated 2026-03-05, inspected ligand sections on pages 45-48 and 60. All four KOJ copies have bond-length and bond-angle outliers; B/C/D torsion outliers; short contacts A:3, B:3, C:1. KOJ A516/B508/C514/D510 RSCC/RSR are 0.82/0.17, 0.86/0.12, 0.86/0.15, 0.88/0.17. Reported ligand geometry/density-fit caveats remain unresolved; no independent map interpretation, distance/contact calculation, protonation, refinement, full side-chain or whole-model quality audit was performed.

Every edge carries its own citation; an uncited edge is refused by the corpus tests.

Causal graph — bioactivity 3 nodes, 2 edges

Deposited kojic-acid associations with two distinct TyrBm constructs, grounded to native B2ZB02 without assigning the reference isolate VS1 to an unspecified structural source strain. DOI:10.1016/j.jmb.2010.10.048 was tool-inaccessible. A partial read of DOI:10.1038/srep34993 stopped at an identity redirect; no alternate retrieval or quantitative functional experiment is adopted. Structural association is not a direct binding assay, measured inhibition, affinity or inhibition mode, physiological metal stoichiometry, cellular phenotype, or a producer/BGC claim. Protein engineering here does not change the natural-product origin classification.

SubjectPredicateObjectNotesEvidence
kojic acid has_deposited_structural_association_with Priestia megaterium TyrBm 1..297 + His6 (3NQ1) Construct-specific association in PDB:3NQ1; canonical UniProt grounds the reference protein, not an assertion that this is the intact native protein. The deposited title is quoted as metadata, not independently verified inhibition or active-site chemistry. Ligand geometry and density-fit limitations are retained in the validation evidence.
https://www.rcsb.org/structure/3NQ1
https://www.uniprot.org/uniprotkb/B2ZB02
https://www.ncbi.nlm.nih.gov/protein/ACC86108.1
https://www.ncbi.nlm.nih.gov/nuccore/EU627691.1
https://data.rcsb.org/rest/v1/core/chemcomp/KOJ
https://files.rcsb.org/validation/view/3nq1_full_validation.pdf
  • reference
    https://www.rcsb.org/structure/3NQ1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Independent curator sequence/model comparison using the deposited reference; quoted titles and source metadata remain attributed to the deposit. PDB revision 1.3, X-ray resolution 2.30 angstrom. 303-aa deposited construct matching native positions 1..297 plus six C-terminal histidines. Modeled author positions A/B 4..286 (283 per chain); the His6 tag is unmodeled. Every modeled polymer residue matches its audited construct; side-chain completeness is not established. Native source Bacillus megaterium, now Priestia megaterium, taxon 1404; PDB source strain unspecified, not assigned VS1. Expression host E. coli taxon 562, BL21(DE3), plasmid pET9d. KOJ A1351/B1351 (label F/Q); four Cu and thirteen Zn ions deposited. Each KOJ has ten heavy atoms at modeled occupancy 1 without alternates. Metal inventory does not establish physiological stoichiometry or coordination.
    snippet
    Crystal Structure of Tyrosinase from Bacillus megaterium in complex with inhibitor kojic acid
  • reference
    https://www.uniprot.org/uniprotkb/B2ZB02
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Unreviewed entry version 78, sequence version 1, Priestia megaterium taxon 1404, 297 aa. No kojic-acid inhibition annotation is present in the inspected entry. The structural construct is grounded by exact sequence correspondence, not by assuming a reviewed status or a convenient tyrosinase homolog.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/ACC86108.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Independent curator sequence/model comparison using the deposited reference; quoted titles and source metadata remain attributed to the deposit. Complete 297-aa native reference, deposited Bacillus megaterium isolate VS1, taxon 1404, matching B2ZB02 exactly. The native isolate is not transferred to the unspecified PDB source strain or identified as the historical assay stock.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/EU627691.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 894-nt CDS 1..894, codon_start 1/table 11, independently translates to 297 aa identical to ACC86108.1 and B2ZB02. The structural tag/truncation is separately resolved against this reference. No complete expression-plasmid DNA or historical assay-stock identity is established.
  • reference
    https://data.rcsb.org/rest/v1/core/chemcomp/KOJ
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    CCD KOJ has neutral charge, C6H6O4, no chiral atoms and the same StandardInChI and InChIKey as CHEBI:43572. This establishes deposited component identity, not protonation or coordination in the metal complex.
  • reference
    https://files.rcsb.org/validation/view/3nq1_full_validation.pdf
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Report dated 2026-03-05, inspected pages 4, 20-21 and 23-24. Each KOJ has six bond-length, six bond-angle, one torsion outlier and six short contacts. KOJ A1351/B1351 RSCC/RSR: 0.82/0.21 and 0.77/0.18. Reported ligand geometry/density-fit caveats remain unresolved; no independent map interpretation, distance/contact calculation, protonation, refinement, full side-chain or whole-model quality audit was performed.
kojic acid has_deposited_structural_association_with Priestia megaterium TyrBm 4..290 (5I38) Construct-specific association in PDB:5I38; canonical UniProt grounds the reference protein, not an assertion that this is the intact native protein. The deposited title is quoted as metadata, not independently verified inhibition or active-site chemistry. Ligand geometry and density-fit limitations are retained in the validation evidence.
https://www.rcsb.org/structure/5I38
https://www.uniprot.org/uniprotkb/B2ZB02
https://www.ncbi.nlm.nih.gov/protein/ACC86108.1
https://www.ncbi.nlm.nih.gov/nuccore/EU627691.1
https://data.rcsb.org/rest/v1/core/chemcomp/KOJ
https://files.rcsb.org/validation/view/5i38_full_validation.pdf
  • reference
    https://www.rcsb.org/structure/5I38
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Independent curator sequence/model comparison using the deposited reference; quoted titles and source metadata remain attributed to the deposit. PDB revision 1.2, X-ray resolution 2.60 angstrom. 287-aa deposited fragment matching native positions 4..290. Modeled author positions A 5..290 and B 4..290 (286/287 residues). Every modeled polymer residue matches its audited construct; side-chain completeness is not established. Native source Bacillus megaterium, now Priestia megaterium, taxon 1404; PDB source strain unspecified, not assigned VS1. Expression host E. coli BL21(DE3) taxon 469008, plasmid pET9D. KOJ A303/B303 (label E/H); four Cu ions deposited. Each KOJ has ten heavy atoms at modeled occupancy 1 without alternates. Metal inventory does not establish physiological stoichiometry or coordination.
    snippet
    Crystal Structure of tyrosinase from Bacillus megaterium with inhibitor kojic acid in the active site
  • reference
    https://www.uniprot.org/uniprotkb/B2ZB02
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Unreviewed entry version 78, sequence version 1, Priestia megaterium taxon 1404, 297 aa. No kojic-acid inhibition annotation is present in the inspected entry. The structural construct is grounded by exact sequence correspondence, not by assuming a reviewed status or a convenient tyrosinase homolog.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/ACC86108.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Independent curator sequence/model comparison using the deposited reference; quoted titles and source metadata remain attributed to the deposit. Complete 297-aa native reference, deposited Bacillus megaterium isolate VS1, taxon 1404, matching B2ZB02 exactly. The native isolate is not transferred to the unspecified PDB source strain or identified as the historical assay stock.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/EU627691.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 894-nt CDS 1..894, codon_start 1/table 11, independently translates to 297 aa identical to ACC86108.1 and B2ZB02. The structural tag/truncation is separately resolved against this reference. No complete expression-plasmid DNA or historical assay-stock identity is established.
  • reference
    https://data.rcsb.org/rest/v1/core/chemcomp/KOJ
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    CCD KOJ has neutral charge, C6H6O4, no chiral atoms and the same StandardInChI and InChIKey as CHEBI:43572. This establishes deposited component identity, not protonation or coordination in the metal complex.
  • reference
    https://files.rcsb.org/validation/view/5i38_full_validation.pdf
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Report dated 2026-03-05, inspected pages 4, 11-12 and 14. Each KOJ has four bond-length and two torsion outliers; A has six and B five bond-angle outliers, neither has short contacts. KOJ A303/B303 RSCC/RSR: 0.81/0.17 and 0.93/0.12. Reported ligand geometry/density-fit caveats remain unresolved; no independent map interpretation, distance/contact calculation, protonation, refinement, full side-chain or whole-model quality audit was performed.

Every edge carries its own citation; an uncited edge is refused by the corpus tests.

Causal graph — biosynthesis 2 nodes, 1 edge

Database-qualified GO annotation of Aspergillus oryzae RIB40 reference protein AO090038000370, putative Hst4, to negative regulation of parent kojic-acid biosynthesis. The exact acts_upstream_of_or_within relation is retained; this does not identify a direct substrate, transcriptional target, biochemical reaction or ordered pathway step. The primary experiment was not independently inspected. No HstD alias, specific mutant phenotype, expression construct, quantitative production effect, BGC membership or producer-grade upgrade is inferred.

SubjectPredicateObjectNotesEvidence
AO090038000370 (putative Hst4; RIB40 reference) acts_upstream_of_or_within negative regulation of kojic acid biosynthetic process Adopted AspGD/QuickGO database annotation, not a newly verified knockout result. IMP/ECO:0000315 is the source evidence code; this edge remains DATABASE_ASSERTION. Reference-sequence comparisons are CURATOR_INFERENCE and support grounding only. The process already denotes negative regulation; no extra direct inhibitory edge or compound-production measurement is asserted.
https://www.ebi.ac.uk/QuickGO/services/annotation/search?geneProductId=UniProtKB%3AQ2U2P7&goId=GO%3A1900395&limit=100
https://www.uniprot.org/uniprotkb/Q2U2P7
https://www.ebi.ac.uk/QuickGO/services/ontology/go/terms/GO%3A1900395
https://www.ncbi.nlm.nih.gov/protein/BAE64168.1
https://www.ncbi.nlm.nih.gov/protein/XP_001825301.3
https://www.ncbi.nlm.nih.gov/nuccore/AP007169.1
https://www.ncbi.nlm.nih.gov/nuccore/XM_001825249.3
  • reference
    https://www.ebi.ac.uk/QuickGO/services/annotation/search?geneProductId=UniProtKB%3AQ2U2P7&goId=GO%3A1900395&limit=100
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Official response has one hit and one page: annotation UniProtKB:Q2U2P7!417351419, symbol AO090038000370, taxon 510516, GO:1900395, qualifier acts_upstream_of_or_within, IMP/ECO:0000315, assignedBy AspGD, annotation date 20130823, reference PMID:23729383, no NOT qualifier or extension. DOI:10.1128/ec.00003-13 remains access-held; no alternate retrieval or independently inspected primary phenotype is adopted.
  • reference
    https://www.uniprot.org/uniprotkb/Q2U2P7
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    Unreviewed entry version 109, sequence version 1, 571 aa; Aspergillus oryzae ATCC 42149 / RIB40 taxon 510516, locus AO090038000370. GO:1900395 carries IMP:AspGD and ECO:0000315/PMID:23729383. Protein existence is inferred from homology, not experimental protein detection. Automated class-I sirtuin annotation disagrees with the deposited NCBI sirtuin-5/class-III annotation; neither class nor direct deacetylase activity is adopted.
    snippet
    P:negative regulation of kojic acid biosynthetic process
  • reference
    https://www.ebi.ac.uk/QuickGO/services/ontology/go/terms/GO%3A1900395
    evidence type
    DATABASE_ASSERTION
    retrieved on
    2026-10-09
    notes
    GO:1900395 is non-obsolete, biological_process, unrestricted. Its kojic-acid process and exact systematic-name synonyms provide the compound context; formula-only related synonyms are not chemical identity proof.
    snippet
    Any process that stops, prevents or reduces the frequency, rate or extent of kojic acid biosynthetic process.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/BAE64168.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 571-aa deposited reference is identical to Q2U2P7. Native Aspergillus oryzae RIB40, taxon 510516, locus AO090038000370, old locus AO070331000235. Sequence equality grounds the reference, not the historical mutant stock, assay protein or expression construct.
  • reference
    https://www.ncbi.nlm.nih.gov/protein/XP_001825301.3
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    The complete 571-aa PROVISIONAL RefSeq is identical to Q2U2P7 and BAE64168.1. Its putative Hst4 label is retained as provisional, not equated with HstD. Same deposited RIB40/taxon 510516/locus metadata; no demonstrated protein activity or experimental stock identity follows.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/AP007169.1
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    Bounded native interval 961433..963216 (1784 nt) contains the complete CDS complement(join(961433..962814,962883..963216)), codon_start 1/default table 1. Independent translation of the 1716-nt spliced CDS is identical to the 571-aa annotation, BAE64168.1 and Q2U2P7. No full scaffold, promoter or experimental construct identity is established.
  • reference
    https://www.ncbi.nlm.nih.gov/nuccore/XM_001825249.3
    evidence type
    CURATOR_INFERENCE
    retrieved on
    2026-10-09
    notes
    PROVISIONAL partial mRNA, incomplete on both ends, with a precise complete CDS 1..1716, codon_start 1/default table 1. Its CDS is nucleotide-identical to the spliced native CDS and independently translates to XP_001825301.3 and Q2U2P7 (571 aa). This does not establish a full transcript or equate whole genomic records.

Every edge carries its own citation; an uncited edge is refused by the corpus tests.

Molecular targets 7

TargetTarget organismMeasurementEvidence
Polyphenol oxidase 1
PROTEIN BINDS
UniProtKB:Q00024		 Agaricus bisporus
NCBITaxon:5341		 IC50 16670 nM
PMID:20476840
  • reference
    PMID:20476840
    evidence type
    DATABASE_ASSERTION
    notes
    BindingDB own-curated affinity; measured at pH 6.8000, 25.00 C C; qualifier EQUAL.
Polyphenol oxidase 1 [61-568]
PROTEIN BINDS
UniProtKB:Q00024		 Agaricus bisporus
NCBITaxon:5341		 IC50 23600 nM
PMID:27669118
  • reference
    PMID:27669118
    evidence type
    DATABASE_ASSERTION
    notes
    BindingDB own-curated affinity; measured at pH 6.8000; qualifier EQUAL.
Polyphenol oxidase 1 [N65D,S176D,K211T,P277A,P406L]
PROTEIN BINDS
UniProtKB:Q00024		 Agaricus bisporus var. bisporus (strain H97 / ATCC MYA-4626 / FGSC 10389)
NCBITaxon:936046		 KI 12200 nM
PMID:26496408
  • reference
    PMID:26496408
    evidence type
    DATABASE_ASSERTION
    notes
    BindingDB own-curated affinity; measured at pH 6.8000; qualifier EQUAL.
Polyphenol oxidase 2
PROTEIN BINDS
UniProtKB:O42713		 Agaricus bisporus
NCBITaxon:5341		 IC50 12500 nM
PMID:18608767
  • reference
    PMID:18608767
    evidence type
    DATABASE_ASSERTION
    notes
    BindingDB own-curated affinity; measured at 30.00 C C; qualifier EQUAL.
Polyphenol oxidase 2
PROTEIN BINDS
UniProtKB:O42713		 Agaricus bisporus
NCBITaxon:5341		 IC50 23000 nM
PMID:23461881
  • reference
    PMID:23461881
    evidence type
    DATABASE_ASSERTION
    notes
    BindingDB own-curated affinity; measured at pH 6.8000, 25.00 C C; qualifier EQUAL.
Tyrosinase
PROTEIN BINDS
UniProtKB:P14679		 Homo sapiens
NCBITaxon:9606		 IC50 16670 nM
PMID:16206837
  • reference
    PMID:16206837
    evidence type
    DATABASE_ASSERTION
    notes
    BindingDB own-curated affinity; measured at pH 6.8000, 37.00 C C; qualifier EQUAL.
Uncharacterized protein YOR062C
PROTEIN BINDS
UniProtKB:P36025		 Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
NCBITaxon:559292		 IC50 19000 nM
PMID:25916324
  • reference
    PMID:25916324
    evidence type
    DATABASE_ASSERTION
    notes
    BindingDB own-curated affinity; measured at pH 6.8000; qualifier EQUAL.

Bioactivities 25

Entries preserve source qualifiers, targets and evidence. Repeated assay names or values are not independent replications; inspect source detail for differences.

AssayResultTarget enzymeSource detail
Cellular viability qHTS for adrenocortical cancer (ACC) cell line NCI-H295ROTHER 4.6109 uM; NOT_DETERMINEDNot recorded
pubchem.aid:1963990
assay
Cellular viability qHTS for adrenocortical cancer (ACC) cell line NCI-H295R
evidence
  • reference
    pubchem.aid:1963990
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1963990, deposited by NCGC; assay type Confirmatory. Source outcome: Inconclusive. Source endpoint: Potency.
call
NOT_DETERMINED
measurement type
OTHER
value
4.6109
units
uM
Enzymatic Activity Assay from Article 10.1016/j.bioorg.2015.10.003: "Development of hydroxylated naphthylchalcones as polyphenol oxidase inhibitors: Synthesis, biochemistry and molecular docking studies."KI 12.2 uM; INACTIVEUniProtKB:Q00024
PMID:26496408
assay
Enzymatic Activity Assay from Article 10.1016/j.bioorg.2015.10.003: "Development of hydroxylated naphthylchalcones as polyphenol oxidase inhibitors: Synthesis, biochemistry and molecular docking studies."
evidence
  • reference
    PMID:26496408
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1801486, deposited by BindingDB; assay type Confirmatory.
call
INACTIVE
measurement type
KI
value
12.2
units
uM
target enzyme
UniProtKB:Q00024
In Vitro Tyrosinase Inhibition Assay from Article 10.3109/14756366.2010.482529: "Tyrosinase inhibitory effect of benzoic acid derivatives and their structure-activity relationships."IC50 16.67 uM; INACTIVEUniProtKB:Q00024
PMID:20476840
assay
In Vitro Tyrosinase Inhibition Assay from Article 10.3109/14756366.2010.482529: "Tyrosinase inhibitory effect of benzoic acid derivatives and their structure-activity relationships."
evidence
  • reference
    PMID:20476840
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1802947, deposited by BindingDB; assay type Confirmatory.
call
INACTIVE
measurement type
IC50
value
16.67
units
uM
target enzyme
UniProtKB:Q00024
Inhibition Assay from Article 10.1080/14756360500179333: "Tyrosinase inhibition: conformational analysis based studies on molecular dynamics calculations of bipiperidine based inhibitors."IC50 16.67 uM; INACTIVEUniProtKB:P14679
PMID:16206837
assay
Inhibition Assay from Article 10.1080/14756360500179333: "Tyrosinase inhibition: conformational analysis based studies on molecular dynamics calculations of bipiperidine based inhibitors."
evidence
  • reference
    PMID:16206837
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1799678, deposited by BindingDB; assay type Confirmatory.
call
INACTIVE
measurement type
IC50
value
16.67
units
uM
target enzyme
UniProtKB:P14679
Inhibition Assay from US Patent US9422261: "Heterocyclic resorcinol derivatives, preparation of same and cosmetic uses thereof"IC50 15 uM; INACTIVEUniProtKB:Q00024
pubchem.aid:1803246
assay
Inhibition Assay from US Patent US9422261: "Heterocyclic resorcinol derivatives, preparation of same and cosmetic uses thereof"
evidence
  • reference
    pubchem.aid:1803246
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1803246, deposited by BindingDB; assay type Confirmatory.
call
INACTIVE
measurement type
IC50
value
15.0
units
uM
target enzyme
UniProtKB:Q00024
Mushroom Tyrosinase Assay from US Patent US9682910: "Series of skin-whitening (lightening) compounds"IC50 20 uM; INACTIVEUniProtKB:Q8R2Y2
pubchem.aid:1794918
assay
Mushroom Tyrosinase Assay from US Patent US9682910: "Series of skin-whitening (lightening) compounds"
evidence
  • reference
    pubchem.aid:1794918
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1794918, deposited by BindingDB; assay type Confirmatory.
call
INACTIVE
measurement type
IC50
value
20.0
units
uM
target enzyme
UniProtKB:Q8R2Y2
NCATS anti-infectives library activity on the primary C. elegans qHTS viability assayOTHER 0.1995 uM; NOT_DETERMINEDNot recorded
PMID:36786055
assay
NCATS anti-infectives library activity on the primary C. elegans qHTS viability assay
evidence
  • reference
    PMID:36786055
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1745855, deposited by NCGC; assay type Confirmatory. Source outcome: Inconclusive. Source endpoint: Potency.
call
NOT_DETERMINED
measurement type
OTHER
value
0.1995
units
uM
Primary qHTS for Inhibitors of N-terminal methyltransferase 1 (NTMT1): MTaseGlo AssayOTHER 0.0447 uM; INACTIVENot recorded
pubchem.aid:1645870
assay
Primary qHTS for Inhibitors of N-terminal methyltransferase 1 (NTMT1): MTaseGlo Assay
evidence
  • reference
    pubchem.aid:1645870
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1645870, deposited by NCGC; assay type Confirmatory. Source endpoint: Potency.
call
INACTIVE
measurement type
OTHER
value
0.0447
units
uM
Primary qHTS for Inhibitors of N-terminal methyltransferase 1 (NTMT1): MTaseGlo AssayOTHER 0.0447 uM; INACTIVEUniProtKB:Q9BV86
pubchem.aid:1645870
assay
Primary qHTS for Inhibitors of N-terminal methyltransferase 1 (NTMT1): MTaseGlo Assay
evidence
  • reference
    pubchem.aid:1645870
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1645870, deposited by NCGC; assay type Confirmatory. Source endpoint: Potency.
call
INACTIVE
measurement type
OTHER
value
0.0447
units
uM
target enzyme
UniProtKB:Q9BV86
Primary qHTS for inhibitors of NSP2Pro chikungunya virus (CHIKV)OTHER 0.0101 uM; NOT_DETERMINEDUniProtKB:Q8JUX6
pubchem.aid:1964107
assay
Primary qHTS for inhibitors of NSP2Pro chikungunya virus (CHIKV)
evidence
  • reference
    pubchem.aid:1964107
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1964107, deposited by NCGC; assay type Confirmatory. Source outcome: Inconclusive. Source endpoint: Potency.
call
NOT_DETERMINED
measurement type
OTHER
value
0.0101
units
uM
target enzyme
UniProtKB:Q8JUX6
Primary qHTS for inhibitors of NSP2Pro chikungunya virus (CHIKV)OTHER 11.0903 uM; NOT_DETERMINEDUniProtKB:Q8JUX6
pubchem.aid:1964107
assay
Primary qHTS for inhibitors of NSP2Pro chikungunya virus (CHIKV)
evidence
  • reference
    pubchem.aid:1964107
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1964107, deposited by NCGC; assay type Confirmatory. Source outcome: Inconclusive. Source endpoint: Potency.
call
NOT_DETERMINED
measurement type
OTHER
value
11.0903
units
uM
target enzyme
UniProtKB:Q8JUX6
Primary qHTS for small molecule stabilizers of the endoplasmic reticulum resident proteome: Secreted ER Calcium Modulated Protein (SERCaMP) assayOTHER 8.9125 uM; NOT_DETERMINEDNot recorded
PMID:33910017
assay
Primary qHTS for small molecule stabilizers of the endoplasmic reticulum resident proteome: Secreted ER Calcium Modulated Protein (SERCaMP) assay
evidence
  • reference
    PMID:33910017
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1508630, deposited by NCGC; assay type Confirmatory. Source outcome: Inconclusive. Source endpoint: Potency.
call
NOT_DETERMINED
measurement type
OTHER
value
8.9125
units
uM
S16 Schwann cell PMP22 intronic element firefly luciferase assayOTHER 16.1366 uM; ACTIVENot recorded
pubchem.aid:624032
assay
S16 Schwann cell PMP22 intronic element firefly luciferase assay
evidence
  • reference
    pubchem.aid:624032
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 624032, deposited by NCGC; assay type Confirmatory. Source endpoint: Potency. Target accession NP_058733 was left ungrounded because PubChem did not provide a UniProtKB accession.
call
ACTIVE
measurement type
OTHER
value
16.1366
units
uM
Spectrophotometric Assay from Article 10.1111/cbdd.12126: "Microwave-assisted synthesis and tyrosinase inhibitory activity of chalcone derivatives."IC50 23 uM; INACTIVEUniProtKB:O42713
PMID:23461881
assay
Spectrophotometric Assay from Article 10.1111/cbdd.12126: "Microwave-assisted synthesis and tyrosinase inhibitory activity of chalcone derivatives."
evidence
  • reference
    PMID:23461881
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1800143, deposited by BindingDB; assay type Confirmatory.
call
INACTIVE
measurement type
IC50
value
23.0
units
uM
target enzyme
UniProtKB:O42713
Tyrosinase Activity Assay from Article 10.1016/j.bioorg.2016.09.007: "Molecular docking studies and biological evaluation of 1,3,4-thiadiazole derivatives bearing Schiff base moieties as tyrosinase inhibitors."IC50 23.6 uM; INACTIVEUniProtKB:Q00024
PMID:27669118
assay
Tyrosinase Activity Assay from Article 10.1016/j.bioorg.2016.09.007: "Molecular docking studies and biological evaluation of 1,3,4-thiadiazole derivatives bearing Schiff base moieties as tyrosinase inhibitors."
evidence
  • reference
    PMID:27669118
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1801979, deposited by BindingDB; assay type Confirmatory.
call
INACTIVE
measurement type
IC50
value
23.6
units
uM
target enzyme
UniProtKB:Q00024
Tyrosinase Assay from Article 10.1080/14756360701810207: "Inhibitory effects on mushroom tyrosinase by flavones from the stem barks of Morus lhou (S.) Koidz."IC50 12.5 uM; INACTIVEUniProtKB:O42713
PMID:18608767
assay
Tyrosinase Assay from Article 10.1080/14756360701810207: "Inhibitory effects on mushroom tyrosinase by flavones from the stem barks of Morus lhou (S.) Koidz."
evidence
  • reference
    PMID:18608767
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1799721, deposited by BindingDB; assay type Confirmatory.
call
INACTIVE
measurement type
IC50
value
12.5
units
uM
target enzyme
UniProtKB:O42713
Tyrosinase Inhibition Assay from Article 10.1111/cbdd.12577: "Synthesis and biological evaluation of kojic acid derivatives containing 1,2,4-triazole as potent tyrosinase inhibitors."IC50 19 uM; INACTIVEUniProtKB:P36025
PMID:25916324
assay
Tyrosinase Inhibition Assay from Article 10.1111/cbdd.12577: "Synthesis and biological evaluation of kojic acid derivatives containing 1,2,4-triazole as potent tyrosinase inhibitors."
evidence
  • reference
    PMID:25916324
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1801390, deposited by BindingDB; assay type Confirmatory.
call
INACTIVE
measurement type
IC50
value
19.0
units
uM
target enzyme
UniProtKB:P36025
Tyrosinase Inhibition Assay from US Patent US10857082: "Diarylalkanes as potent inhibitors of binuclear enzymes"IC50 29 uM; INACTIVEUniProtKB:Q00024
pubchem.aid:1805056
assay
Tyrosinase Inhibition Assay from US Patent US10857082: "Diarylalkanes as potent inhibitors of binuclear enzymes"
evidence
  • reference
    pubchem.aid:1805056
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1805056, deposited by BindingDB; assay type Confirmatory.
call
INACTIVE
measurement type
IC50
value
29.0
units
uM
target enzyme
UniProtKB:Q00024
qHTS Assay for Identifying Compounds that block Entry of Ebola Virus, Screen 2 blue channelOTHER 8.9125 uM; INACTIVENot recorded
pubchem.aid:1117304
assay
qHTS Assay for Identifying Compounds that block Entry of Ebola Virus, Screen 2 blue channel
evidence
  • reference
    pubchem.aid:1117304
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1117304, deposited by NCGC; assay type Confirmatory. Source endpoint: AC50.
call
INACTIVE
measurement type
OTHER
value
8.9125
units
uM
qHTS Assay for Identifying Compounds that block Entry of Ebola Virus, Screen 2 green channelOTHER 0.7079 uM; INACTIVENot recorded
pubchem.aid:1117298
assay
qHTS Assay for Identifying Compounds that block Entry of Ebola Virus, Screen 2 green channel
evidence
  • reference
    pubchem.aid:1117298
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1117298, deposited by NCGC; assay type Confirmatory. Source endpoint: AC50.
call
INACTIVE
measurement type
OTHER
value
0.7079
units
uM
qHTS Assay for Identifying Compounds that block Entry of Ebola Virus, Screen 2 ratio channelOTHER 8.9125 uM; INACTIVENot recorded
pubchem.aid:1117305
assay
qHTS Assay for Identifying Compounds that block Entry of Ebola Virus, Screen 2 ratio channel
evidence
  • reference
    pubchem.aid:1117305
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1117305, deposited by NCGC; assay type Confirmatory. Source endpoint: AC50.
call
INACTIVE
measurement type
OTHER
value
8.9125
units
uM
qHTS Assay for Identifying Compounds that block Entry of Ebola Virus: Screen 2, blue channelOTHER 8.91251 uM; INACTIVENot recorded
pubchem.aid:1117314
assay
qHTS Assay for Identifying Compounds that block Entry of Ebola Virus: Screen 2, blue channel
evidence
  • reference
    pubchem.aid:1117314
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1117314, deposited by NCGC; assay type Confirmatory. Source endpoint: Ac50.
call
INACTIVE
measurement type
OTHER
value
8.91251
units
uM
qHTS Assay for Identifying Compounds that block Entry of Ebola Virus: Screen 2, green channelOTHER 0.707946 uM; INACTIVENot recorded
pubchem.aid:1117310
assay
qHTS Assay for Identifying Compounds that block Entry of Ebola Virus: Screen 2, green channel
evidence
  • reference
    pubchem.aid:1117310
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1117310, deposited by NCGC; assay type Confirmatory. Source endpoint: Ac50.
call
INACTIVE
measurement type
OTHER
value
0.707946
units
uM
qHTS Assay for Identifying Compounds that block Entry of Ebola Virus: Screen2, ratio channelOTHER 8.91251 uM; INACTIVENot recorded
pubchem.aid:1117312
assay
qHTS Assay for Identifying Compounds that block Entry of Ebola Virus: Screen2, ratio channel
evidence
  • reference
    pubchem.aid:1117312
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 1117312, deposited by NCGC; assay type Confirmatory. Source endpoint: Ac50.
call
INACTIVE
measurement type
OTHER
value
8.91251
units
uM
qHTS Assay for Inhibitors of Human Jumonji Domain Containing 2E (JMJD2E)OTHER 25.1189 uM; ACTIVENot recorded
pubchem.aid:2147
assay
qHTS Assay for Inhibitors of Human Jumonji Domain Containing 2E (JMJD2E)
evidence
  • reference
    pubchem.aid:2147
    evidence type
    DATABASE_ASSERTION
    notes
    PubChem BioAssay AID 2147, deposited by NCGC; assay type Confirmatory. Source endpoint: Potency. Target accession 2W2I_A was left ungrounded because PubChem did not provide a UniProtKB accession.
call
ACTIVE
measurement type
OTHER
value
25.1189
units
uM
activity class
ENZYME_INHIBITOR
notes
13 further PubChem assay results are in data/raw/pubchem_bioassay.tsv but not written here.

Explore across X-Mech

AntibioticMech (kojic acid) ↗ MediaIngredientMech (CHEBI:43572) ↗ TaxonMech: Aspergillus oryzae RIB40 (NCBITaxon:510516) ↗ PathwayMech (mibig:BGC0002195) ↗

Provenance

Source conceptSourceVersion
BGC0002195MIBIG2
CHEBI:43572CHEBI3-star

This page is generated from data/natural_products/polyketides/kojic-acid.yaml, which is generated from the committed inventories. Neither is edited by hand.