Enzyme

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     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
ID:1.14.13.92
Description:Phenylacetone monooxygenase.
Alternative Name: PAMO.
Cath: 3.50.50.60;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.13.92
BRENDA Enzyme Link: BRENDA 1.14.13.92
KEGG Enzyme Link: KEGG1.14.13.92
BioCyc Enzyme Link: BioCyc 1.14.13.92
ExPASy Enzyme Link: ExPASy1.14.13.92
EC2PDB Enzyme Link: EC2PDB 1.14.13.92
ExplorEnz Enzyme Link: ExplorEnz 1.14.13.92
PRIAM enzyme-specific profiles Link: PRIAM 1.14.13.92
IntEnz Enzyme Link: IntEnz 1.14.13.92
MEDLINE Enzyme Link: MEDLINE 1.14.13.92
MSA:

1.14.13.92;

Phylogenetic Tree:

1.14.13.92;

Uniprot:
M-CSA:
RHEA:10124 H(+) + NADPH + O2 + phenylacetone = benzyl acetate + H2O + NADP(+)
RULE(radius=1) [*:1]-[N;H0;+0:2]1-[CH;+0:3]=[C;H0;+0:4](-[*:5])-[CH2;+0:6]-[CH;+0:7]=[CH;+0:8]-1.[*:9]=[C;H0;+0:10](-[*:11])-[CH2;+0:12]-[*:13].[H+;H0:14].[O;H0;+0:15]=[O;H0;+0:16]>>[*:1]-[n+;H0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[*:9]=[C;H0;+0:10](-[*:11])-[O;H0;+0:15]-[CH2;+0:12]-[*:13].[OH2;+0:16]
Reaction
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References

TitleAuthorsDatePubMed ID
Kinetic mechanism of phenylacetone monooxygenase from Thermobifida fusca.Torres Pazmiño DE, Baas BJ, Janssen DB, Fraaije MW2008 Apr 118321069
Discovery of a thermostable Baeyer-Villiger monooxygenase by genome mining.Fraaije MW, Wu J, Heuts DP, van Hellemond EW, Spelberg JH, Janssen DB2005 Jan15599520
Crystal structure of a Baeyer-Villiger monooxygenase.Malito E, Alfieri A, Fraaije MW, Mattevi A2004 Sep 715328411