NaturalProductMech

anditomin

CHEBI:219836 EXACT SEEDED

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REVIEWED records curator sign-off on identity, structure, filing class and producer claims; DEPRECATED retains a superseded or out-of-scope record.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 meroterpenoid with formula C25H30O5. It is isolated from the fungus Aspergillus stellatus.

Structure

Standard InChIKey	HWLYZRWDCDSFFO-VIJQBOBYSA-N
SMILES	C=C1C2C(=O)[C@]3(C)C[C@@H]4C(=O)OC[C@]14[C@@]1(CC[C@H]4C(C)(C)OC(=O)C=C[C@]4(C)[C@H]21)C3
Stereochemistry	undefined stereocentres — the InChIKey does not distinguish this compound from its stereoisomers
Cross-references	pubchem:91820511, npatlas:NPA032767

Filing pathway

Unclassified — 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 terpene, 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.

Taxon	Basis	Cluster	Evidence
Aspergillus stellatus NCBITaxon:1549217	SOURCE_ASSERTION	mibig:BGC0002612	PMID:25216349

Occurrences 1

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.

Taxon	Source	Reference
Aspergillus stellatus NCBITaxon:1549217	CHEBI	10.1039/c39810000914

Biosynthetic gene clusters 1

Accession	Host	Locus evidence	Genome
mibig:BGC0002612	Aspergillus stellatus NCBITaxon:1549217	CLUSTER_DEMONSTRATED	genbank:AB981314.1

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

Causal graph — biosynthesis 3 nodes, 2 edges

Aspergillus stellatus AndF-catalyzed oxidative rearrangement of andilesin C to anditomin.

Subject	Predicate	Object	Notes	Evidence
andilesin C	is oxidatively rearranged by	AndF dioxygenase	AndF performs the terminal oxidative rearrangement that converts andilesin C into anditomin.	DOI:10.1021/ja508127q https://mite.lisc.univie.ac.at/repository/MITE0000361 https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk https://www.uniprot.org/uniprotkb/A0A097ZPD9 https://www.ncbi.nlm.nih.gov/protein/BAP81860.1 reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT snippet Another dioxygenase, AndF, is also responsible for the structural complexification, generating the end product anditomin by an oxidative rearrangement. notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and assigned AndF as the dioxygenase that oxidatively rearranges the terminal andilesin intermediate to anditomin. reference https://mite.lisc.univie.ac.at/repository/MITE0000361 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes MITE0000361 is active and links AndF to UniProtKB:A0A097ZPD9, GenPept BAP81860.1, MIBiG BGC0002612 and the in vitro conversion of andilesin C into final anditomin by oxidative rearrangement. reference https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes MIBiG BGC0002612.3 places BAP81860.1 in the active Aspergillus stellatus anditomin biosynthetic gene cluster as the AndF 2OG-Fe(II)-dependent dioxygenase. reference https://www.uniprot.org/uniprotkb/A0A097ZPD9 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes Reviewed UniProtKB:A0A097ZPD9 is the 285 aa Emericella variicolor, also Aspergillus stellatus, dioxygenase AndF entry and cross-references EMBL AB981314 protein BAP81860.1. reference https://www.ncbi.nlm.nih.gov/protein/BAP81860.1 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes NCBI GenPept BAP81860.1 is the Aspergillus stellatus AndF protein encoded on AB981314.1:9234..10091.
AndF dioxygenase	forms	anditomin	The MITE reaction and PubMed abstract both describe anditomin as the final product of the AndF-dependent oxidative rearrangement.	DOI:10.1021/ja508127q reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT snippet Another dioxygenase, AndF, is also responsible for the structural complexification, generating the end product anditomin by an oxidative rearrangement. notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and assigned AndF as the dioxygenase that oxidatively rearranges the terminal andilesin intermediate to anditomin.

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

Causal graph — biosynthesis 3 nodes, 2 edges

Aspergillus stellatus AndH-catalyzed reduction of andilesin B to andilesin C.

Subject	Predicate	Object	Notes	Evidence
andilesin B	is reduced by	AndH short-chain dehydrogenase/reductase	AndH reduces the meroterpenoid intermediate andilesin B in the andilesin branch of the anditomin pathway.	DOI:10.1021/ja508127q https://mite.lisc.univie.ac.at/repository/MITE0000360 https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk https://www.uniprot.org/uniprotkb/A0A097ZPD4 https://www.ncbi.nlm.nih.gov/protein/BAP81862.1 reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000360 and UniProtKB:A0A097ZPD4 both cite this paper for the AndH reduction step in the andilesin branch. reference https://mite.lisc.univie.ac.at/repository/MITE0000360 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes MITE0000360 is active and links AndH to UniProtKB:A0A097ZPD4, GenPept BAP81862.1 and MIBiG BGC0002612 for heterologous-expression evidence of the conversion of andilesin B to andilesin C. reference https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes MIBiG BGC0002612.3 places BAP81862.1 in the active Aspergillus stellatus anditomin biosynthetic gene cluster as the AndH short-chain dehydrogenase/reductase. reference https://www.uniprot.org/uniprotkb/A0A097ZPD4 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes Reviewed UniProtKB:A0A097ZPD4 is the 337 aa Emericella variicolor, also Aspergillus stellatus, oxidoreductase AndH entry and cross-references EMBL AB981314 protein BAP81862.1. reference https://www.ncbi.nlm.nih.gov/protein/BAP81862.1 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes NCBI GenPept BAP81862.1 is the Aspergillus stellatus AndH protein encoded on AB981314.1:12753..13104 and AB981314.1:13154..13815.
AndH short-chain dehydrogenase/reductase	forms	andilesin C	MITE0000360 describes AndH-dependent conversion of andilesin B to andilesin C.	DOI:10.1021/ja508127q reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000360 and UniProtKB:A0A097ZPD4 both cite this paper for the AndH reduction step in the andilesin branch.

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

Causal graph — biosynthesis 3 nodes, 2 edges

Aspergillus stellatus AndI-catalyzed reduction of andilesin D to andilesin A.

Subject	Predicate	Object	Notes	Evidence
andilesin D	is reduced by	AndI short-chain dehydrogenase	AndI reduces the meroterpenoid intermediate andilesin D in the andilesin branch of the anditomin pathway.	DOI:10.1021/ja508127q https://mite.lisc.univie.ac.at/repository/MITE0000358 https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk https://www.uniprot.org/uniprotkb/A0A097ZPE8 https://www.ncbi.nlm.nih.gov/protein/BAP81863.1 reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000358 and UniProtKB:A0A097ZPE8 both cite this paper for the AndI reduction step in the andilesin branch. reference https://mite.lisc.univie.ac.at/repository/MITE0000358 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes MITE0000358 is active and links AndI to UniProtKB:A0A097ZPE8, GenPept BAP81863.1 and MIBiG BGC0002612 for heterologous-expression evidence of the conversion of andilesin D to andilesin A. reference https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes MIBiG BGC0002612.3 places BAP81863.1 in the active Aspergillus stellatus anditomin biosynthetic gene cluster as the AndI short-chain dehydrogenase/reductase. reference https://www.uniprot.org/uniprotkb/A0A097ZPE8 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes Reviewed UniProtKB:A0A097ZPE8 is the 290 aa Emericella variicolor, also Aspergillus stellatus, short-chain dehydrogenase AndI entry and cross-references EMBL AB981314 protein BAP81863.1. reference https://www.ncbi.nlm.nih.gov/protein/BAP81863.1 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes NCBI GenPept BAP81863.1 is the Aspergillus stellatus AndI protein encoded on AB981314.1:14876..14897 and AB981314.1:14946..15796.
AndI short-chain dehydrogenase	forms	andilesin A	MITE0000358 describes AndI-dependent conversion of andilesin D to andilesin A.	DOI:10.1021/ja508127q reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000358 and UniProtKB:A0A097ZPE8 both cite this paper for the AndI reduction step in the andilesin branch.

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

Causal graph — biosynthesis 3 nodes, 2 edges

Aspergillus stellatus AndG-catalyzed O-acetylation of andilesin A to O-acetylandilesin A.

Subject	Predicate	Object	Notes	Evidence
andilesin A	is O-acetylated by	AndG O-acetyltransferase	AndG O-acetylates andilesin A in the andilesin branch of the anditomin pathway.	DOI:10.1021/ja508127q https://mite.lisc.univie.ac.at/repository/MITE0000359 https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk https://www.uniprot.org/uniprotkb/A0A097ZPE2 https://www.ncbi.nlm.nih.gov/protein/BAP81861.1 reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000359 and UniProtKB:A0A097ZPE2 both cite this paper for the AndG O-acetylation step in the andilesin branch. reference https://mite.lisc.univie.ac.at/repository/MITE0000359 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 snippet Acetylates andilesin A at the C-6' hydroxyl group position, leading to an instable intermediate that eventually results in andilesin B. notes MITE0000359 is active and links AndG to UniProtKB:A0A097ZPE2, GenPept BAP81861.1 and MIBiG BGC0002612 for O-acetylation of andilesin A. reference https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes MIBiG BGC0002612.3 places BAP81861.1 in the active Aspergillus stellatus anditomin biosynthetic gene cluster as the AndG acetyltransferase. reference https://www.uniprot.org/uniprotkb/A0A097ZPE2 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes Reviewed UniProtKB:A0A097ZPE2 is the 481 aa Emericella variicolor, also Aspergillus stellatus, O-acetyltransferase AndG entry and cross-references EMBL AB981314 protein BAP81861.1. reference https://www.ncbi.nlm.nih.gov/protein/BAP81861.1 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes NCBI GenPept BAP81861.1 is the Aspergillus stellatus AndG protein encoded on complement(AB981314.1:10918..12363).
AndG O-acetyltransferase	forms	O-acetylandilesin A	MITE0000359 describes AndG-dependent acetylation of andilesin A to an unstable O-acetylated intermediate.	DOI:10.1021/ja508127q reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000359 and UniProtKB:A0A097ZPE2 both cite this paper for the AndG O-acetylation step in the andilesin branch.

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

Causal graph — biosynthesis 3 nodes, 2 edges

Aspergillus stellatus AndJ-catalyzed Baeyer-Villiger oxidation of andiconin to andilesin D.

Subject	Predicate	Object	Notes	Evidence
andiconin	is Baeyer-Villiger oxidized by	AndJ FAD-binding monooxygenase	AndJ oxidizes the meroterpenoid intermediate andiconin in the andilesin branch of the anditomin pathway.	DOI:10.1021/ja508127q https://mite.lisc.univie.ac.at/repository/MITE0000357 https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk https://www.uniprot.org/uniprotkb/A0A097ZPG2 https://www.ncbi.nlm.nih.gov/protein/BAP81864.1 reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000357 and UniProtKB:A0A097ZPG2 both cite this paper for the AndJ Baeyer-Villiger oxidation step in the andilesin branch. reference https://mite.lisc.univie.ac.at/repository/MITE0000357 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 snippet Conversion of andiconin to andilesin D by introduction of a lacton ring.. notes MITE0000357 is active and links AndJ to UniProtKB:A0A097ZPG2, GenPept BAP81864.1 and MIBiG BGC0002612 for Baeyer-Villiger oxidation of andiconin to andilesin D. reference https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes MIBiG BGC0002612.3 places BAP81864.1 in the active Aspergillus stellatus anditomin biosynthetic gene cluster as the AndJ FAD-dependent monooxygenase. reference https://www.uniprot.org/uniprotkb/A0A097ZPG2 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes Reviewed UniProtKB:A0A097ZPG2 is the 633 aa Emericella variicolor, also Aspergillus stellatus, FAD-binding monooxygenase AndJ entry and cross-references EMBL AB981314 protein BAP81864.1. reference https://www.ncbi.nlm.nih.gov/protein/BAP81864.1 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes NCBI GenPept BAP81864.1 is the Aspergillus stellatus AndJ protein encoded on complement(AB981314.1:15881..17782).
AndJ FAD-binding monooxygenase	forms	andilesin D	MITE0000357 describes AndJ-dependent Baeyer-Villiger oxidation of andiconin to andilesin D.	DOI:10.1021/ja508127q reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000357 and UniProtKB:A0A097ZPG2 both cite this paper for the AndJ Baeyer-Villiger oxidation step in the andilesin branch.

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

Causal graph — biosynthesis 3 nodes, 2 edges

Aspergillus stellatus AndA-catalyzed structural rearrangement of preandiloid C to andiconin.

Subject	Predicate	Object	Notes	Evidence
preandiloid C	is structurally rearranged by	AndA dioxygenase	AndA catalyzes the structural rearrangement of preandiloid C to generate the bicyclo[2.2.2]octane core in the anditomin pathway.	DOI:10.1021/ja508127q https://mite.lisc.univie.ac.at/repository/MITE0000356 https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk https://www.uniprot.org/uniprotkb/A0A097ZPD5 https://www.ncbi.nlm.nih.gov/protein/BAP81855.1 reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000356 and UniProtKB:A0A097ZPD5 both cite this paper for the AndA structural rearrangement of preandiloid C to andiconin. reference https://mite.lisc.univie.ac.at/repository/MITE0000356 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 snippet Conversion of preandiloid C to andiconin. notes MITE0000356 is active and links AndA to UniProtKB:A0A097ZPD5, GenPept BAP81855.1 and MIBiG BGC0002612 for in vitro and heterologous-expression evidence of structural rearrangement from preandiloid C to andiconin. reference https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes MIBiG BGC0002612.3 places BAP81855.1 in the active Aspergillus stellatus anditomin biosynthetic gene cluster as the AndA 2OG-Fe(II)-dependent dioxygenase. reference https://www.uniprot.org/uniprotkb/A0A097ZPD5 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes Reviewed UniProtKB:A0A097ZPD5 is the 293 aa Emericella variicolor, also Aspergillus stellatus, dioxygenase AndA entry and cross-references EMBL AB981314 protein BAP81855.1. reference https://www.ncbi.nlm.nih.gov/protein/BAP81855.1 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes NCBI GenPept BAP81855.1 is the Aspergillus stellatus AndA protein encoded on complement(AB981314.1:101..982).
AndA dioxygenase	forms	andiconin	MITE0000356 describes AndA-dependent cyclization of preandiloid C to andiconin.	DOI:10.1021/ja508127q reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000356 and UniProtKB:A0A097ZPD5 both cite this paper for the AndA structural rearrangement of preandiloid C to andiconin.

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

Causal graph — biosynthesis 3 nodes, 2 edges

Aspergillus stellatus AndK-catalyzed hydroxylation of DMOA in the anditomin biosynthetic pathway.

Subject	Predicate	Object	Notes	Evidence
3,5-dimethylorsellinic acid	is hydroxylated by	AndK cytochrome P450	AndK catalyzes the first hydroxylation of DMOA in the anditomin pathway.	DOI:10.1021/ja508127q https://mite.lisc.univie.ac.at/repository/MITE0000351 https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk https://www.uniprot.org/uniprotkb/A0A097ZPE4 https://www.ncbi.nlm.nih.gov/protein/BAP81865.1 reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000351 and UniProtKB:A0A097ZPE4 both cite this paper for AndK conversion of DMOA toward DHDMP. reference https://mite.lisc.univie.ac.at/repository/MITE0000351 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 snippet Hydroxylation as the first step in the anditomin biosynthetic pathway. notes MITE0000351 is active and links AndK to UniProtKB:A0A097ZPE4, GenPept BAP81865.1 and MIBiG BGC0002612 for heterologous-expression evidence of the first AndK hydroxylation reaction from DMOA to hydroxymethylated DMOA. reference https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes MIBiG BGC0002612.3 places BAP81865.1 in the active Aspergillus stellatus anditomin biosynthetic gene cluster as the AndK cytochrome P450 monooxygenase/hydrolase. reference https://www.uniprot.org/uniprotkb/A0A097ZPE4 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes Reviewed UniProtKB:A0A097ZPE4 is the 865 aa Emericella variicolor, also Aspergillus stellatus, cytochrome P450 monooxygenase AndK entry and cross-references EMBL AB981314 protein BAP81865.1. reference https://www.ncbi.nlm.nih.gov/protein/BAP81865.1 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes NCBI GenPept BAP81865.1 is the Aspergillus stellatus AndK protein encoded on AB981314.1 exons 18286..21221.
AndK cytochrome P450	forms	2,4-dihydroxy-6-(hydroxymethyl)-3,5-dimethylbenzoic acid	MITE0000351 describes AndK-dependent hydroxylation of DMOA to hydroxymethylated DMOA before AndK-dependent cyclization to DHDMP.	DOI:10.1021/ja508127q reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000351 and UniProtKB:A0A097ZPE4 both cite this paper for AndK conversion of DMOA toward DHDMP.

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

Causal graph — biosynthesis 3 nodes, 2 edges

Aspergillus stellatus AndK-catalyzed cyclization of hydroxymethylated DMOA to DHDMP.

Subject	Predicate	Object	Notes	Evidence
2,4-dihydroxy-6-(hydroxymethyl)-3,5-dimethylbenzoic acid	is cyclized by	AndK cytochrome P450	AndK catalyzes cyclization of hydroxymethylated DMOA to DHDMP as the second AndK-dependent step of anditomin biosynthesis.	DOI:10.1021/ja508127q https://mite.lisc.univie.ac.at/repository/MITE0000351 https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk https://www.uniprot.org/uniprotkb/A0A097ZPE4 https://www.ncbi.nlm.nih.gov/protein/BAP81865.1 reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. assigned AndK as the Aspergillus stellatus enzyme converting DMOA through hydroxymethylated DMOA to DHDMP. reference https://mite.lisc.univie.ac.at/repository/MITE0000351 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 snippet Cyclization as second step in the anditomin biosynthetic pathway. notes MITE0000351 links A0A097ZPE4, BAP81865.1 and BGC0002612 to the second AndK cyclization. reference https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk evidence type DATABASE_ASSERTION retrieved on 2026-10-01 reference https://www.uniprot.org/uniprotkb/A0A097ZPE4 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 reference https://www.ncbi.nlm.nih.gov/protein/BAP81865.1 evidence type DATABASE_ASSERTION retrieved on 2026-10-01
AndK cytochrome P450	forms	5,7-dihydroxy-4,6-dimethylphthalide	MITE0000351 describes AndK-dependent cyclization of the hydroxymethylated DMOA intermediate to form the phthalide DHDMP before AndD prenylation.	DOI:10.1021/ja508127q reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT

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

Causal graph — biosynthesis 3 nodes, 2 edges

Aspergillus stellatus AndD-catalyzed prenylation of DHDMP in the anditomin biosynthetic pathway.

Subject	Predicate	Object	Notes	Evidence
5,7-dihydroxy-4,6-dimethylphthalide	is prenylated by	AndD prenyltransferase	AndD prenylates DHDMP in the anditomin pathway before AndE epoxidation of the farnesylated product.	DOI:10.1021/ja508127q https://mite.lisc.univie.ac.at/repository/MITE0000352 https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk https://www.uniprot.org/uniprotkb/A0A097ZPE3 https://www.ncbi.nlm.nih.gov/protein/BAP81858.1 reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000352 and UniProtKB:A0A097ZPE3 both cite this paper for AndD prenylation of DHDMP to farnesyl-DHDMP. reference https://mite.lisc.univie.ac.at/repository/MITE0000352 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 snippet Prenylation as the third step in the anditomin biosynthetic pathway. notes MITE0000352 is active and links AndD to UniProtKB:A0A097ZPE3, GenPept BAP81858.1 and MIBiG BGC0002612 for heterologous-expression evidence of DHDMP prenylation to farnesyl-DHDMP. reference https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes MIBiG BGC0002612.3 places BAP81858.1 in the active Aspergillus stellatus anditomin biosynthetic gene cluster as the AndD prenyltransferase. reference https://www.uniprot.org/uniprotkb/A0A097ZPE3 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes Reviewed UniProtKB:A0A097ZPE3 is the 327 aa Emericella variicolor, also Aspergillus stellatus, polyprenyl transferase AndD entry and cross-references EMBL AB981314 protein BAP81858.1. reference https://www.ncbi.nlm.nih.gov/protein/BAP81858.1 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes NCBI GenPept BAP81858.1 is the Aspergillus stellatus AndD protein encoded on complement(AB981314.1:4149..5132).
AndD prenyltransferase	forms	farnesyl-DHDMP	MITE0000352 describes AndD-dependent prenylation of DHDMP to generate farnesyl-DHDMP.	DOI:10.1021/ja508127q reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000352 and UniProtKB:A0A097ZPE3 both cite this paper for AndD prenylation of DHDMP to farnesyl-DHDMP.

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

Causal graph — biosynthesis 3 nodes, 2 edges

Aspergillus stellatus AndE-catalyzed epoxidation of farnesyl-DHDMP in the anditomin biosynthetic pathway.

Subject	Predicate	Object	Notes	Evidence
farnesyl-DHDMP	is epoxidized by	AndE FAD-dependent monooxygenase	AndE epoxidizes farnesyl-DHDMP in the anditomin pathway before AndB cyclization of the epoxidized product.	DOI:10.1021/ja508127q https://mite.lisc.univie.ac.at/repository/MITE0000353 https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk https://www.uniprot.org/uniprotkb/A0A097ZPF7 https://www.ncbi.nlm.nih.gov/protein/BAP81859.1 reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000353 and UniProtKB:A0A097ZPF7 both cite this paper for AndE epoxidation of farnesyl-DHDMP to epoxyfarnesyl-DHDMP. reference https://mite.lisc.univie.ac.at/repository/MITE0000353 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 snippet Epoxidation of farnesyl-DHDMP to give epoxyfarnesyl-DHDMP in the anditomin biosynthetic pathway. notes MITE0000353 is active and links AndE to UniProtKB:A0A097ZPF7, GenPept BAP81859.1 and MIBiG BGC0002612 for heterologous-expression evidence of farnesyl-DHDMP epoxidation to epoxyfarnesyl-DHDMP. reference https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes MIBiG BGC0002612.3 places BAP81859.1 in the active Aspergillus stellatus anditomin biosynthetic gene cluster as the AndE FAD-dependent monooxygenase. reference https://www.uniprot.org/uniprotkb/A0A097ZPF7 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes Reviewed UniProtKB:A0A097ZPF7 is the 471 aa Emericella variicolor, also Aspergillus stellatus, FAD-dependent monooxygenase AndE entry and cross-references EMBL AB981314 protein BAP81859.1. reference https://www.ncbi.nlm.nih.gov/protein/BAP81859.1 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes NCBI GenPept BAP81859.1 is the Aspergillus stellatus AndE protein encoded on complement(AB981314.1:5331..6894).
AndE FAD-dependent monooxygenase	forms	epoxyfarnesyl-DHDMP	MITE0000353 describes AndE-dependent conversion of farnesyl-DHDMP to epoxyfarnesyl-DHDMP.	DOI:10.1021/ja508127q reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000353 and UniProtKB:A0A097ZPF7 both cite this paper for AndE epoxidation of farnesyl-DHDMP to epoxyfarnesyl-DHDMP.

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

Causal graph — biosynthesis 3 nodes, 2 edges

Aspergillus stellatus AndB-catalyzed cyclization of epoxyfarnesyl-DHDMP to preandiloid A.

Subject	Predicate	Object	Notes	Evidence
epoxyfarnesyl-DHDMP	is cyclized by	AndB terpene cyclase	AndB opens the epoxide ring and cyclizes the farnesyl moiety of epoxyfarnesyl-DHDMP to form preandiloid A before AndC oxidation.	DOI:10.1021/ja508127q https://mite.lisc.univie.ac.at/repository/MITE0000354 https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk https://www.uniprot.org/uniprotkb/A0A097ZPD8 https://www.ncbi.nlm.nih.gov/protein/BAP81856.1 reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000354 and UniProtKB:A0A097ZPD8 both cite this paper for AndB cyclization of epoxyfarnesyl-DHDMP to preandiloid A. reference https://mite.lisc.univie.ac.at/repository/MITE0000354 evidence type DATABASE_ASSERTION retrieved on 2026-10-02 snippet Converts epoxyfarnesyl-DHDMP to preandiloid A. notes MITE0000354 is active and links AndB to UniProtKB:A0A097ZPD8, GenPept BAP81856.1 and MIBiG BGC0002612 for heterologous-expression evidence of epoxyfarnesyl-DHDMP cyclization to preandiloid A. reference https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk evidence type DATABASE_ASSERTION retrieved on 2026-10-02 notes MIBiG BGC0002612.3 places BAP81856.1 in the active Aspergillus stellatus anditomin biosynthetic gene cluster as the AndB terpene cyclase. reference https://www.uniprot.org/uniprotkb/A0A097ZPD8 evidence type DATABASE_ASSERTION retrieved on 2026-10-02 notes Reviewed UniProtKB:A0A097ZPD8 is the 236 aa Emericella variicolor, also Aspergillus stellatus, terpene cyclase AndB entry and cross-references EMBL AB981314 protein BAP81856.1. reference https://www.ncbi.nlm.nih.gov/protein/BAP81856.1 evidence type DATABASE_ASSERTION retrieved on 2026-10-02 notes NCBI GenPept BAP81856.1 is the Aspergillus stellatus AndB protein encoded on AB981314.1:1720..2222 and AB981314.1:2294..2501.
AndB terpene cyclase	forms	preandiloid A	MITE0000354 describes AndB-dependent conversion of epoxyfarnesyl-DHDMP to preandiloid A.	DOI:10.1021/ja508127q reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000354 and UniProtKB:A0A097ZPD8 both cite this paper for AndB cyclization of epoxyfarnesyl-DHDMP to preandiloid A.

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

Causal graph — biosynthesis 3 nodes, 2 edges

Aspergillus stellatus AndC-catalyzed oxidation of preandiloid A to preandiloid B.

Subject	Predicate	Object	Notes	Evidence
preandiloid A	is oxidized by	AndC short-chain dehydrogenase	AndC oxidizes the C-3 hydroxyl of preandiloid A to form preandiloid B before separate AndA-catalyzed dehydrogenation.	DOI:10.1021/ja508127q https://mite.lisc.univie.ac.at/repository/MITE0000355 https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk https://www.uniprot.org/uniprotkb/A0A097ZPC9 https://www.ncbi.nlm.nih.gov/protein/BAP81857.1 reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000355 and UniProtKB:A0A097ZPC9 both cite this paper for AndC oxidation of preandiloid A to preandiloid B. reference https://mite.lisc.univie.ac.at/repository/MITE0000355 evidence type DATABASE_ASSERTION retrieved on 2026-10-02 snippet Conversion of preandiloid A at C-3 hydroxyl to give preandiloid B. notes MITE0000355 is active and links AndC to UniProtKB:A0A097ZPC9, GenPept BAP81857.1 and MIBiG BGC0002612 for heterologous-expression evidence of C-3 hydroxyl oxidation of preandiloid A to preandiloid B. reference https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk evidence type DATABASE_ASSERTION retrieved on 2026-10-02 notes MIBiG BGC0002612.3 places BAP81857.1 in the active Aspergillus stellatus anditomin biosynthetic gene cluster as the AndC short-chain dehydrogenase/reductase. reference https://www.uniprot.org/uniprotkb/A0A097ZPC9 evidence type DATABASE_ASSERTION retrieved on 2026-10-02 notes Reviewed UniProtKB:A0A097ZPC9 is the 252 aa Emericella variicolor, also Aspergillus stellatus, short-chain dehydrogenase AndC entry and cross-references EMBL AB981314 protein BAP81857.1. reference https://www.ncbi.nlm.nih.gov/protein/BAP81857.1 evidence type DATABASE_ASSERTION retrieved on 2026-10-02 notes NCBI GenPept BAP81857.1 is the Aspergillus stellatus AndC protein encoded on AB981314.1:3007..3027, AB981314.1:3087..3525, AB981314.1:3581..3658 and AB981314.1:3726..3946.
AndC short-chain dehydrogenase	forms	preandiloid B	MITE0000355 describes AndC-dependent conversion of preandiloid A to preandiloid B.	DOI:10.1021/ja508127q reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000355 and UniProtKB:A0A097ZPC9 both cite this paper for AndC oxidation of preandiloid A to preandiloid B.

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

Causal graph — biosynthesis 3 nodes, 2 edges

Aspergillus stellatus AndA-catalyzed dehydrogenation of preandiloid B to preandiloid C.

Subject	Predicate	Object	Notes	Evidence
preandiloid B	is dehydrogenated by	AndA dioxygenase	AndA dehydrogenates preandiloid B to yield the enone preandiloid C before its separate AndA-catalyzed structural rearrangement.	DOI:10.1021/ja508127q https://mite.lisc.univie.ac.at/repository/MITE0000356 https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk https://www.uniprot.org/uniprotkb/A0A097ZPD5 https://www.ncbi.nlm.nih.gov/protein/BAP81855.1 reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000356 and UniProtKB:A0A097ZPD5 both cite this paper for AndA dehydrogenation of preandiloid B to preandiloid C. reference https://mite.lisc.univie.ac.at/repository/MITE0000356 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 snippet Conversion of preandiloid B yielding the enone preandiloid C. notes MITE0000356 is active and links AndA to UniProtKB:A0A097ZPD5, GenPept BAP81855.1 and MIBiG BGC0002612 for in vitro and heterologous-expression evidence of dehydrogenation from preandiloid B to preandiloid C. reference https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes MIBiG BGC0002612.3 places BAP81855.1 in the active Aspergillus stellatus anditomin biosynthetic gene cluster as the AndA 2OG-Fe(II)-dependent dioxygenase. reference https://www.uniprot.org/uniprotkb/A0A097ZPD5 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes Reviewed UniProtKB:A0A097ZPD5 is the 293 aa Emericella variicolor, also Aspergillus stellatus, dioxygenase AndA entry and cross-references EMBL AB981314 protein BAP81855.1. reference https://www.ncbi.nlm.nih.gov/protein/BAP81855.1 evidence type DATABASE_ASSERTION retrieved on 2026-10-01 notes NCBI GenPept BAP81855.1 is the Aspergillus stellatus AndA protein encoded on complement(AB981314.1:101..982).
AndA dioxygenase	forms	preandiloid C	MITE0000356 describes AndA-dependent dehydrogenation of preandiloid B to preandiloid C.	DOI:10.1021/ja508127q reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster and experimentally assigned its dedicated enzymes; MITE0000356 and UniProtKB:A0A097ZPD5 both cite this paper for AndA dehydrogenation of preandiloid B to preandiloid C.

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

Causal graph — biosynthesis 5 nodes, 4 edges

Aspergillus stellatus AndM-catalyzed polyketide synthesis of DMOA in the anditomin biosynthetic pathway.

Subject	Predicate	Object	Notes	Evidence
acetyl-CoA	supplies the starter unit to	AndM non-reducing polyketide synthase	RHEA:49628 consumes one acetyl-CoA as the starter unit for AndM-catalyzed 3,5-dimethylorsellinate synthesis.	DOI:10.1021/ja508127q https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk https://www.uniprot.org/uniprotkb/A0A097ZPE0 https://ftp.expasy.org/databases/rhea/tsv/rhea2uniprot_sprot.tsv reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster; UniProtKB:A0A097ZPE0 cites this paper for the first pathway step, AndM synthesis of 3,5-dimethylorsellinic acid. reference https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk evidence type DATABASE_ASSERTION retrieved on 2026-10-02 notes MIBiG BGC0002612.3 places BAP81867.1 in the active Aspergillus stellatus anditomin biosynthetic gene cluster as the AndM polyketide synthase. reference https://www.uniprot.org/uniprotkb/A0A097ZPE0 evidence type DATABASE_ASSERTION retrieved on 2026-10-02 notes Reviewed UniProtKB:A0A097ZPE0 is the 2,430 aa Emericella variicolor, also Aspergillus stellatus, non-reducing polyketide synthase AndM entry; it cross-references EMBL AB981314 protein BAP81867.1 and assigns the RHEA:49628 3,5-dimethylorsellinate-forming reaction to AndM. reference https://ftp.expasy.org/databases/rhea/tsv/rhea2uniprot_sprot.tsv evidence type DATABASE_ASSERTION retrieved on 2026-10-02 notes The Rhea-to-UniProtKB Swiss-Prot mapping links RHEA:49628, the 3,5-dimethylorsellinate-forming reaction from malonyl-CoA, acetyl-CoA and S-adenosyl-L-methionine, to UniProtKB:A0A097ZPE0.
malonyl-CoA	supplies extender units to	AndM non-reducing polyketide synthase	RHEA:49628 consumes three malonyl-CoA units for AndM-catalyzed 3,5-dimethylorsellinate synthesis.	DOI:10.1021/ja508127q https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk https://www.uniprot.org/uniprotkb/A0A097ZPE0 https://ftp.expasy.org/databases/rhea/tsv/rhea2uniprot_sprot.tsv reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster; UniProtKB:A0A097ZPE0 cites this paper for the first pathway step, AndM synthesis of 3,5-dimethylorsellinic acid. reference https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk evidence type DATABASE_ASSERTION retrieved on 2026-10-02 notes MIBiG BGC0002612.3 places BAP81867.1 in the active Aspergillus stellatus anditomin biosynthetic gene cluster as the AndM polyketide synthase. reference https://www.uniprot.org/uniprotkb/A0A097ZPE0 evidence type DATABASE_ASSERTION retrieved on 2026-10-02 notes Reviewed UniProtKB:A0A097ZPE0 is the 2,430 aa Emericella variicolor, also Aspergillus stellatus, non-reducing polyketide synthase AndM entry; it cross-references EMBL AB981314 protein BAP81867.1 and assigns the RHEA:49628 3,5-dimethylorsellinate-forming reaction to AndM. reference https://ftp.expasy.org/databases/rhea/tsv/rhea2uniprot_sprot.tsv evidence type DATABASE_ASSERTION retrieved on 2026-10-02 notes The Rhea-to-UniProtKB Swiss-Prot mapping links RHEA:49628, the 3,5-dimethylorsellinate-forming reaction from malonyl-CoA, acetyl-CoA and S-adenosyl-L-methionine, to UniProtKB:A0A097ZPE0.
S-adenosyl-L-methionine	supplies methyl groups to	AndM non-reducing polyketide synthase	RHEA:49628 consumes two S-adenosyl-L-methionine molecules for AndM-catalyzed methylation during 3,5-dimethylorsellinate synthesis.	DOI:10.1021/ja508127q https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk https://www.uniprot.org/uniprotkb/A0A097ZPE0 https://ftp.expasy.org/databases/rhea/tsv/rhea2uniprot_sprot.tsv reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster; UniProtKB:A0A097ZPE0 cites this paper for the first pathway step, AndM synthesis of 3,5-dimethylorsellinic acid. reference https://mibig.secondarymetabolites.org/repository/BGC0002612.3/BGC0002612.gbk evidence type DATABASE_ASSERTION retrieved on 2026-10-02 notes MIBiG BGC0002612.3 places BAP81867.1 in the active Aspergillus stellatus anditomin biosynthetic gene cluster as the AndM polyketide synthase. reference https://www.uniprot.org/uniprotkb/A0A097ZPE0 evidence type DATABASE_ASSERTION retrieved on 2026-10-02 notes Reviewed UniProtKB:A0A097ZPE0 is the 2,430 aa Emericella variicolor, also Aspergillus stellatus, non-reducing polyketide synthase AndM entry; it cross-references EMBL AB981314 protein BAP81867.1 and assigns the RHEA:49628 3,5-dimethylorsellinate-forming reaction to AndM. reference https://ftp.expasy.org/databases/rhea/tsv/rhea2uniprot_sprot.tsv evidence type DATABASE_ASSERTION retrieved on 2026-10-02 notes The Rhea-to-UniProtKB Swiss-Prot mapping links RHEA:49628, the 3,5-dimethylorsellinate-forming reaction from malonyl-CoA, acetyl-CoA and S-adenosyl-L-methionine, to UniProtKB:A0A097ZPE0.
AndM non-reducing polyketide synthase	forms	3,5-dimethylorsellinic acid	AndM catalyzes the first anditomin pathway step, producing the DMOA scaffold later hydroxylated and cyclized by AndK.	DOI:10.1021/ja508127q reference DOI:10.1021/ja508127q evidence type PRIMARY_EXPERIMENT notes Matsuda et al. identified the Aspergillus stellatus anditomin biosynthetic gene cluster; UniProtKB:A0A097ZPE0 cites this paper for the first pathway step, AndM synthesis of 3,5-dimethylorsellinic acid.

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

Explore across X-Mech

AntibioticMech (anditomin) ↗ MediaIngredientMech (CHEBI:219836) ↗ TaxonMech: Aspergillus stellatus (NCBITaxon:1549217) ↗ PathwayMech (mibig:BGC0002612) ↗

Provenance

Source concept	Source	Version
BGC0002612	MIBIG	3
CHEBI:219836	CHEBI	3-star

This page is generated from data/natural_products/unclassified/anditomin.yaml, which is generated from the committed inventories. Neither is edited by hand.