phenylethylamine degradation II

MetaCyc:PWY-6534

The complete native two-reaction route converts 2-phenylethylamine through phenylacetaldehyde to phenylacetate in Pseudomonas putida strain U. The CTQ-containing PeaACD quinohaemoprotein dehydrogenase uses an external electron acceptor, unlike the copper/TPQ oxidase of degradation I. The complete Rhea equation retains the generic A/AH2 redox couple; it does not identify a strain-U physiological acceptor. Azurin-like carrier reconstitution used P. putida IFO 15366, and cytochrome c550 experiments used Paracoccus, so neither is substituted here. PeaACD composition and cofactor assignments are source-curated, with the strain-U heterotrimer assignment described as in silico in BRENDA. PeaB supports enzyme maturation/activity rather than serving as a fourth catalytic subunit. The NAD-dependent PeaE activity is retained without fixing its oligomeric state: native MetaCyc annotates a homodimer, whereas later secondary literature describes a PeaEFG complex. PeaE is not the only possible aldehyde-oxidizing activity; its deletion retains activity and growth, and PeaF/G are proposed contributors whose exact catalytic chemistry is not resolved here. This record does not claim that the listed proteins alone reconstitute strain-U growth. Transport, cofactor maturation, respiratory-chain regeneration and downstream phenylacetate assimilation lie outside the two native reactions. The 2008 strain-U primary abstract was inspected; its full body was unavailable, so detailed database statements are not presented as directly inspected primary results.

Pathway type

aromatic amine degradation

Organism scope

Pseudomonas putida NCBITaxon:303

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Pathway network

22 nodes · 24 asserted directed edges

Arrows show recorded subject → object relationships, not necessarily metabolic flow. Select a node for details or an arrow for evidence. Scroll, zoom or find a node to explore.

Reaction / activity
Chemical / cofactor
Protein / complex
Taxon
Pathway
Solid arrow: mechanistic relation
Dashed arrow: membership, location or cofactor relation

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Components and activities

Declared biological components and source reaction directions
Node	Kind or role	Source direction
Pseudomonas putida `NCBITaxon:303`	taxon
2-phenylethanaminium `CHEBI:225237`	small molecule
hydrogen acceptor `CHEBI:13193`	small molecule
water `CHEBI:15377`	small molecule
phenylacetaldehyde `CHEBI:16424`	small molecule
hydrogen donor `CHEBI:17499`	small molecule
ammonium `CHEBI:28938`	small molecule
NAD(1-) `CHEBI:57540`	small molecule
phenylacetate `CHEBI:18401`	small molecule
NADH(2-) `CHEBI:57945`	small molecule
hydron `CHEBI:15378`	small molecule
PeaA `UniProtKB:B1N7H2`	protein
PeaD `UniProtKB:B1N7G9`	protein
PeaC `UniProtKB:B1N7H0`	protein
PeaB `UniProtKB:B1N7H1`	protein
PeaE `UniProtKB:B1N7H3`	protein
quinohaemoprotein amine dehydrogenase `MetaCyc:CPLX-8088`	complex
cysteine tryptophylquinone residue `CHEBI:20252`	cofactor
heme `CHEBI:30413`	cofactor
2-phenylethylamine + A + H2O => 2-phenylacetaldehyde + AH2 + NH4(+) `RHEA:36724`	molecular activity	left to right
2-phenylacetaldehyde + NAD(+) + H2O => 2-phenylacetate + NADH + 2 H(+) `RHEA:21393`	molecular activity	left to right

Mechanistic edges

Mechanistic edges and their cited evidence
Subject	Predicate and description	Object	Evidence
2-phenylethanaminium `CHEBI:225237`	consumes	2-phenylethylamine + A + H2O => 2-phenylacetaldehyde + AH2 + NH4(+) `RHEA:36724`	RHEA:36724 Source assertion: The directed Rhea reaction places CHEBI:225237 on its substrates side with coefficient 1. Source location `http://rdf.rhea-db.org/36724/rh:substrates -> http://rdf.rhea-db.org/36723_L/rh:contains1 -> http://rdf.rhea-db.org/Participant_36723_compound_4466/rh:compound -> http://rdf.rhea-db.org/Compound_4466/rh:chebi`
hydrogen acceptor `CHEBI:13193`	consumes	2-phenylethylamine + A + H2O => 2-phenylacetaldehyde + AH2 + NH4(+) `RHEA:36724`	RHEA:36724 Source assertion: The directed Rhea reaction places CHEBI:13193 on its substrates side with coefficient 1. Source location `http://rdf.rhea-db.org/36724/rh:substrates -> http://rdf.rhea-db.org/36723_L/rh:contains1 -> http://rdf.rhea-db.org/Participant_36723_compound_3512/rh:compound -> http://rdf.rhea-db.org/Compound_3512/rh:chebi`
water `CHEBI:15377`	consumes	2-phenylethylamine + A + H2O => 2-phenylacetaldehyde + AH2 + NH4(+) `RHEA:36724`	RHEA:36724 Source assertion: The directed Rhea reaction places CHEBI:15377 on its substrates side with coefficient 1. Source location `http://rdf.rhea-db.org/36724/rh:substrates -> http://rdf.rhea-db.org/36723_L/rh:contains1 -> http://rdf.rhea-db.org/Participant_36723_compound_1283/rh:compound -> http://rdf.rhea-db.org/Compound_1283/rh:chebi`
2-phenylethylamine + A + H2O => 2-phenylacetaldehyde + AH2 + NH4(+) `RHEA:36724`	produces	phenylacetaldehyde `CHEBI:16424`	RHEA:36724 Source assertion: The directed Rhea reaction places CHEBI:16424 on its products side with coefficient 1. Source location `http://rdf.rhea-db.org/36724/rh:products -> http://rdf.rhea-db.org/36723_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_36723_compound_2222/rh:compound -> http://rdf.rhea-db.org/Compound_2222/rh:chebi`
2-phenylethylamine + A + H2O => 2-phenylacetaldehyde + AH2 + NH4(+) `RHEA:36724`	produces	hydrogen donor `CHEBI:17499`	RHEA:36724 Source assertion: The directed Rhea reaction places CHEBI:17499 on its products side with coefficient 1. Source location `http://rdf.rhea-db.org/36724/rh:products -> http://rdf.rhea-db.org/36723_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_36723_compound_1304/rh:compound -> http://rdf.rhea-db.org/Compound_1304/rh:chebi`
2-phenylethylamine + A + H2O => 2-phenylacetaldehyde + AH2 + NH4(+) `RHEA:36724`	produces	ammonium `CHEBI:28938`	RHEA:36724 Source assertion: The directed Rhea reaction places CHEBI:28938 on its products side with coefficient 1. Source location `http://rdf.rhea-db.org/36724/rh:products -> http://rdf.rhea-db.org/36723_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_36723_compound_1012/rh:compound -> http://rdf.rhea-db.org/Compound_1012/rh:chebi`
phenylacetaldehyde `CHEBI:16424`	consumes	2-phenylacetaldehyde + NAD(+) + H2O => 2-phenylacetate + NADH + 2 H(+) `RHEA:21393`	RHEA:21393 Source assertion: The directed Rhea reaction places CHEBI:16424 on its substrates side with coefficient 1. Source location `http://rdf.rhea-db.org/21393/rh:substrates -> http://rdf.rhea-db.org/21392_L/rh:contains1 -> http://rdf.rhea-db.org/Participant_21392_compound_2222/rh:compound -> http://rdf.rhea-db.org/Compound_2222/rh:chebi`
NAD(1-) `CHEBI:57540`	consumes	2-phenylacetaldehyde + NAD(+) + H2O => 2-phenylacetate + NADH + 2 H(+) `RHEA:21393`	RHEA:21393 Source assertion: The directed Rhea reaction places CHEBI:57540 on its substrates side with coefficient 1. Source location `http://rdf.rhea-db.org/21393/rh:substrates -> http://rdf.rhea-db.org/21392_L/rh:contains1 -> http://rdf.rhea-db.org/Participant_21392_compound_3484/rh:compound -> http://rdf.rhea-db.org/Compound_3484/rh:chebi`
water `CHEBI:15377`	consumes	2-phenylacetaldehyde + NAD(+) + H2O => 2-phenylacetate + NADH + 2 H(+) `RHEA:21393`	RHEA:21393 Source assertion: The directed Rhea reaction places CHEBI:15377 on its substrates side with coefficient 1. Source location `http://rdf.rhea-db.org/21393/rh:substrates -> http://rdf.rhea-db.org/21392_L/rh:contains1 -> http://rdf.rhea-db.org/Participant_21392_compound_1283/rh:compound -> http://rdf.rhea-db.org/Compound_1283/rh:chebi`
2-phenylacetaldehyde + NAD(+) + H2O => 2-phenylacetate + NADH + 2 H(+) `RHEA:21393`	produces	phenylacetate `CHEBI:18401`	RHEA:21393 Source assertion: The directed Rhea reaction places CHEBI:18401 on its products side with coefficient 1. Source location `http://rdf.rhea-db.org/21393/rh:products -> http://rdf.rhea-db.org/21392_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_21392_compound_5243/rh:compound -> http://rdf.rhea-db.org/Compound_5243/rh:chebi`
2-phenylacetaldehyde + NAD(+) + H2O => 2-phenylacetate + NADH + 2 H(+) `RHEA:21393`	produces	NADH(2-) `CHEBI:57945`	RHEA:21393 Source assertion: The directed Rhea reaction places CHEBI:57945 on its products side with coefficient 1. Source location `http://rdf.rhea-db.org/21393/rh:products -> http://rdf.rhea-db.org/21392_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_21392_compound_1650/rh:compound -> http://rdf.rhea-db.org/Compound_1650/rh:chebi`
2-phenylacetaldehyde + NAD(+) + H2O => 2-phenylacetate + NADH + 2 H(+) `RHEA:21393`	produces	hydron `CHEBI:15378`	RHEA:21393 Source assertion: The directed Rhea reaction places CHEBI:15378 on its products side with coefficient 2. Source location `http://rdf.rhea-db.org/21393/rh:products -> http://rdf.rhea-db.org/21392_R/rh:contains2 -> http://rdf.rhea-db.org/Participant_21392_compound_3249/rh:compound -> http://rdf.rhea-db.org/Compound_3249/rh:chebi`
quinohaemoprotein amine dehydrogenase `MetaCyc:CPLX-8088`	catalyzes Source-curated activity association. This does not claim that strain-U complex stoichiometry was measured by purification or crystallography.	2-phenylethylamine + A + H2O => 2-phenylacetaldehyde + AH2 + NH4(+) `RHEA:36724`	MetaCyc:CPLX-8088 Source assertion: The strain-U quinohaemoprotein complex is annotated as the enzyme of ENZRXN-17923, which points to RXN-11510. Source location `Protein[@frameid="CPLX-8088"]/catalyzes/Enzymatic-Reaction[@frameid="ENZRXN-17923"]/reaction` MetaCyc:RXN-11510 Source assertion: RXN-11510 is explicitly unified with forward RHEA:36724 and is annotated LEFT-TO-RIGHT. Source location `Reaction[@frameid="RXN-11510"]/dblink[dblink-db="RHEA"]; reaction-direction`
PeaE `UniProtKB:B1N7H3`	enables Functional gene-product/activity association only: neither an active isolated monomer nor a fixed PeaE or PeaEFG stoichiometry is asserted. Alternative aldehyde oxidation remains possible.	2-phenylacetaldehyde + NAD(+) + H2O => 2-phenylacetate + NADH + 2 H(+) `RHEA:21393`	MetaCyc:CPLX-8089 Source assertion: The native source assigns the strain-U peaE product to NAD-dependent phenylacetaldehyde dehydrogenase activity and reports retained activity and growth after peaE deletion. Source location `Protein[@frameid="CPLX-8089"]/comment; catalyzes/Enzymatic-Reaction[@frameid="ENZRXN-17924"]/reaction` MetaCyc:MONOMER-15732 Source assertion: The native PeaE polypeptide is explicitly unified with UniProtKB:B1N7H3 and is a component of CPLX-8089. Source location `Protein[@frameid="MONOMER-15732"]/synonym; component-of; dblink[dblink-db="UNIPROT"]` MetaCyc:PHENDEHYD-RXN Source assertion: PHENDEHYD-RXN is annotated REVERSIBLE and cross-references bidirectional RHEA:21395. Source location `Reaction[@frameid="PHENDEHYD-RXN"]/reaction-direction; dblink[dblink-db="RHEA"]` RHEA:21393 Source assertion: Master RHEA:21392 links to forward RHEA:21393 and bidirectional RHEA:21395. Source location `http://rdf.rhea-db.org/21392/rh:directionalReaction -> http://rdf.rhea-db.org/21393; rh:bidirectionalReaction -> http://rdf.rhea-db.org/21395`
quinohaemoprotein amine dehydrogenase `MetaCyc:CPLX-8088`	has_part Native annotated composition, supported at an in silico/source-curation tier; not direct strain-U structural stoichiometry evidence.	PeaA `UniProtKB:B1N7H2`	MetaCyc:CPLX-8088 Source assertion: The native complex annotates one MONOMER-15729 component (PeaA); this is a curated composition assignment. Source location `Protein[@frameid="CPLX-8088"]/component[Protein/@frameid="MONOMER-15729"]/coefficient` MetaCyc:MONOMER-15729 Source assertion: The native polypeptide explicitly unifies MONOMER-15729 with UniProtKB:B1N7H2. Source location `Protein[@frameid="MONOMER-15729"]/dblink[dblink-db="UNIPROT"]` DOI:10.1111/j.1462-2920.2007.01464.x Source assertion: BRENDA describes the strain-U heterotrimer assignment as determined by in silico experiments. Source location `BRENDA reference 686425; Subunits table; EC 1.4.9.1; heterotrimer row`
quinohaemoprotein amine dehydrogenase `MetaCyc:CPLX-8088`	has_part Native annotated composition, supported at an in silico/source-curation tier; not direct strain-U structural stoichiometry evidence.	PeaD `UniProtKB:B1N7G9`	MetaCyc:CPLX-8088 Source assertion: The native complex annotates one MONOMER-15730 component (PeaD); this is a curated composition assignment. Source location `Protein[@frameid="CPLX-8088"]/component[Protein/@frameid="MONOMER-15730"]/coefficient` MetaCyc:MONOMER-15730 Source assertion: The native polypeptide explicitly unifies MONOMER-15730 with UniProtKB:B1N7G9. Source location `Protein[@frameid="MONOMER-15730"]/dblink[dblink-db="UNIPROT"]` DOI:10.1111/j.1462-2920.2007.01464.x Source assertion: BRENDA describes the strain-U heterotrimer assignment as determined by in silico experiments. Source location `BRENDA reference 686425; Subunits table; EC 1.4.9.1; heterotrimer row`
quinohaemoprotein amine dehydrogenase `MetaCyc:CPLX-8088`	has_part Native annotated composition, supported at an in silico/source-curation tier; not direct strain-U structural stoichiometry evidence.	PeaC `UniProtKB:B1N7H0`	MetaCyc:CPLX-8088 Source assertion: The native complex annotates one MONOMER-15731 component (PeaC); this is a curated composition assignment. Source location `Protein[@frameid="CPLX-8088"]/component[Protein/@frameid="MONOMER-15731"]/coefficient` MetaCyc:MONOMER-15731 Source assertion: The native polypeptide explicitly unifies MONOMER-15731 with UniProtKB:B1N7H0. Source location `Protein[@frameid="MONOMER-15731"]/dblink[dblink-db="UNIPROT"]` DOI:10.1111/j.1462-2920.2007.01464.x Source assertion: BRENDA describes the strain-U heterotrimer assignment as determined by in silico experiments. Source location `BRENDA reference 686425; Subunits table; EC 1.4.9.1; heterotrimer row`
PeaB `UniProtKB:B1N7H1`	enables Accessory activity/maturation requirement; not a fourth structural subunit, an individually sufficient catalyst, or a fully specified maturation reaction.	quinohaemoprotein amine dehydrogenase `MetaCyc:CPLX-8088`	MetaCyc:CPLX-8088 Source assertion: The native source reports that peaB knockout mutations render the quinohaemoprotein enzyme inactive. Source location `Protein[@frameid="CPLX-8088"]/comment, second paragraph` UniProtKB:B1N7H1 Source assertion: This sequence entry identifies peaB, protein ABR57203.1, from the strain-U nucleotide-sequence submission associated with PMID18177365. Source location `genes/geneName; references[citation/id="18177365"]/referenceComments[type="STRAIN"]; uniProtKBCrossReferences[database="EMBL"]` DOI:10.1111/j.1462-2920.2007.01464.x Source assertion: BRENDA identifies PeaB as needed for correct function and post-translational modification of the gamma subunit, not an interacting component during catalytic turnover. Source location `BRENDA reference 686425; Subunits table; EC 1.4.9.1; additional information row`
quinohaemoprotein amine dehydrogenase `MetaCyc:CPLX-8088`	has_cofactor Covalently integrated residue, not a freely consumed metabolite. The free CTQ compound CHEBI:73670 linked by old MetaCyc is not substituted for the bound residue.	cysteine tryptophylquinone residue `CHEBI:20252`	MetaCyc:PWY-6534 Source assertion: The native pathway describes its quinohaemoprotein amine dehydrogenase as using cysteine tryptophylquinone (CTQ). Source location `Pathway[@frameid="PWY-6534"]/comment, first paragraph` DOI:10.1111/j.1462-2920.2007.01464.x Source assertion: BRENDA annotates CTQ as a redox cofactor of this enzyme. Source location `BRENDA reference 686425; Cofactor table; EC 1.4.9.1` CHEBI:20252 Source assertion: ChEBI defines this entity as an amino-acid residue derived from cysteine tryptophylquinone. Source location `CHEBI:20252; rdfs:label; IAO:0000115` PMID:22235135 Source assertion: The Introduction identifies CTQ as a post-translationally derived gamma-subunit cofactor of QHNDH. The experiments in this paper concern P. denitrificans Pd1222, not strain U. Source location `PMC3307263; Introduction (sec1), first paragraph; Experimental Procedures (sec2), Materials and Bacterial Strains`
quinohaemoprotein amine dehydrogenase `MetaCyc:CPLX-8088`	has_cofactor Source-curated cofactor assignment; generic heme class preserves the unspecified iron oxidation state. No strain-U experimental stoichiometry measurement is claimed.	heme `CHEBI:30413`	DOI:10.1111/j.1462-2920.2007.01464.x Source assertion: BRENDA annotates two hemes acting as redox-active groups in addition to CTQ. Source location `BRENDA reference 686425; Cofactor table; EC 1.4.9.1; cysteine tryptophylquinone row`
2-phenylethylamine + A + H2O => 2-phenylacetaldehyde + AH2 + NH4(+) `RHEA:36724`	part_of	`MetaCyc:PWY-6534`	MetaCyc:PWY-6534 Source assertion: The complete native reaction-list includes RXN-11510; its pathway layout selects the left-to-right catabolic direction. Source location `Pathway[@frameid="PWY-6534"]/reaction-list; reaction-layout[Reaction/@frameid="RXN-11510"]` MetaCyc:RXN-11510 Source assertion: RXN-11510 is explicitly unified with forward RHEA:36724 and is annotated LEFT-TO-RIGHT. Source location `Reaction[@frameid="RXN-11510"]/dblink[dblink-db="RHEA"]; reaction-direction`
2-phenylacetaldehyde + NAD(+) + H2O => 2-phenylacetate + NADH + 2 H(+) `RHEA:21393`	part_of	`MetaCyc:PWY-6534`	MetaCyc:PWY-6534 Source assertion: The complete native reaction-list includes PHENDEHYD-RXN; its pathway layout selects the left-to-right catabolic direction. Source location `Pathway[@frameid="PWY-6534"]/reaction-list; reaction-layout[Reaction/@frameid="PHENDEHYD-RXN"]` MetaCyc:PHENDEHYD-RXN Source assertion: PHENDEHYD-RXN is annotated REVERSIBLE and cross-references bidirectional RHEA:21395. Source location `Reaction[@frameid="PHENDEHYD-RXN"]/reaction-direction; dblink[dblink-db="RHEA"]` RHEA:21393 Source assertion: Master RHEA:21392 links to forward RHEA:21393 and bidirectional RHEA:21395. Source location `http://rdf.rhea-db.org/21392/rh:directionalReaction -> http://rdf.rhea-db.org/21393; rh:bidirectionalReaction -> http://rdf.rhea-db.org/21395`
2-phenylethylamine + A + H2O => 2-phenylacetaldehyde + AH2 + NH4(+) `RHEA:36724`	provides_input_for	2-phenylacetaldehyde + NAD(+) + H2O => 2-phenylacetate + NADH + 2 H(+) `RHEA:21393`	MetaCyc:PWY-6534 Source assertion: The native pathway orders RXN-11510 before PHENDEHYD-RXN through phenylacetaldehyde. Source location `Pathway[@frameid="PWY-6534"]/reaction-ordering; reaction-layout` RHEA:36724 Source assertion: The directed Rhea reaction places CHEBI:16424 on its products side with coefficient 1. Source location `http://rdf.rhea-db.org/36724/rh:products -> http://rdf.rhea-db.org/36723_R/rh:contains1 -> http://rdf.rhea-db.org/Participant_36723_compound_2222/rh:compound -> http://rdf.rhea-db.org/Compound_2222/rh:chebi` RHEA:21393 Source assertion: The directed Rhea reaction places CHEBI:16424 on its substrates side with coefficient 1. Source location `http://rdf.rhea-db.org/21393/rh:substrates -> http://rdf.rhea-db.org/21392_L/rh:contains1 -> http://rdf.rhea-db.org/Participant_21392_compound_2222/rh:compound -> http://rdf.rhea-db.org/Compound_2222/rh:chebi`
`MetaCyc:PWY-6534`	part_of Strain U is the experimental scope. Species-level identifier does not assert equivalent pathway function in all P. putida strains.	Pseudomonas putida `NCBITaxon:303`	PMID:18177365 Source assertion: The inspected primary abstract reports the strain-U Pea route: phenylethylamine transport, quinohaemoprotein-mediated deamination to phenylacetaldehyde, then oxidation to phenylacetate. Source location `resultList/result[id="18177365"]/abstractText` UniProtKB:B1N7H2 Source assertion: The sequence entry identifies Pseudomonas putida, NCBI taxon 303, and identifies strain U for the original nucleotide-sequence reference. Source location `organism/taxonId; references[citation/id="18177365"]/referenceComments[type="STRAIN"]`

References

RHEA:36724 Rhea directed reaction 36724 (source version: Rhea 142; release 2026-09-02; digest covers complete official RDF gzip; exact selected objects in evidence locators)
RHEA:21393 Rhea directed reaction 21393 (source version: Rhea 142; release 2026-09-02; digest covers complete official RDF gzip; exact selected objects in evidence locators)
MetaCyc:PWY-6534 MetaCyc native PWY-6534 (source version: MetaCyc 22.5 native XML; retrieved 2026-10-11; digest covers the complete response body)
MetaCyc:RXN-11510 MetaCyc native RXN-11510 (source version: MetaCyc 22.5 native XML; retrieved 2026-10-11; digest covers the complete response body)
MetaCyc:PHENDEHYD-RXN MetaCyc native PHENDEHYD-RXN (source version: MetaCyc 22.5 native XML; retrieved 2026-10-11; digest covers the complete response body)
MetaCyc:CPLX-8088 MetaCyc native CPLX-8088 (source version: MetaCyc 22.5 native XML; retrieved 2026-10-11; digest covers the complete response body)
MetaCyc:CPLX-8089 MetaCyc native CPLX-8089 (source version: MetaCyc 22.5 native XML; retrieved 2026-10-11; digest covers the complete response body)
MetaCyc:MONOMER-15729 MetaCyc native MONOMER-15729 (source version: MetaCyc 22.5 native XML; retrieved 2026-10-11; digest covers the complete response body)
MetaCyc:MONOMER-15730 MetaCyc native MONOMER-15730 (source version: MetaCyc 22.5 native XML; retrieved 2026-10-11; digest covers the complete response body)
MetaCyc:MONOMER-15731 MetaCyc native MONOMER-15731 (source version: MetaCyc 22.5 native XML; retrieved 2026-10-11; digest covers the complete response body)
MetaCyc:MONOMER-15732 MetaCyc native MONOMER-15732 (source version: MetaCyc 22.5 native XML; retrieved 2026-10-11; digest covers the complete response body)
UniProtKB:B1N7H1 UniProtKB B1N7H1 unreviewed sequence identity (source version: UniProt 2026_03, released 2026-09-02; full individual JSON retrieved 2026-10-11; not a reviewed experimental catalytic annotation)
UniProtKB:B1N7H2 UniProtKB B1N7H2 unreviewed sequence identity (source version: UniProt 2026_03, released 2026-09-02; full individual JSON retrieved 2026-10-11; not a reviewed experimental catalytic annotation)
PMID:18177365 Genetic analyses and molecular characterization of the pathways involved in the conversion of 2-phenylethylamine and 2-phenylethanol into phenylacetic acid in Pseudomonas putida U. (source version: 2008 primary publication; inspected Europe PMC core metadata and abstract only, retrieved 2026-10-11)
DOI:10.1111/j.1462-2920.2007.01464.x BRENDA annotations of Arias et al. (2008), reference 686425; not primary full text (source version: BRENDA release 2026.1 (March 2026), source-specific tables retrieved 2026-10-11; DOI identifies the annotated publication; digest covers the BRENDA HTML, not the paper)
CHEBI:20252 ChEBI cysteine tryptophylquinone residue (source version: ChEBI 255; digest covers the full uncompressed SemanticSQL database, not the issuing webpage; exact label/definition locators queried 2026-10-11)
PMID:22235135 An Unusual Subtilisin-like Serine Protease Is Essential for Biogenesis of Quinohemoprotein Amine Dehydrogenase (source version: 2012 primary full HTML inspected; used for protein-derived cofactor class and comparative biogenesis scope, not strain-U experimental confirmation; retrieved 2026-10-11)

Curation history

2026-10-11T04:37:11Z Codex
- CREATE — Add the complete two-reaction phenylethylamine degradation II route.
  Retain the Pseudomonas putida strain-U scope, generic native electron acceptor equation, predicted PeaACD composition and unresolved PeaE/F/G assembly physiology. Exact source dossiers and author checks are in research/pathway_additions/2026-10-11-next-189. Independent scientific reviews and shared validation are recorded separately.
Read this curation session