Enzyme

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EC Tree
     1. Oxidoreductases
        1.1 Acting on the CH-OH group of donors
            1.1.3 With oxygen as acceptor
ID:1.1.3.38
Description:Vanillyl-alcohol oxidase.
Alternative Name: 4-hydroxy-2-methoxybenzyl alcohol oxidase.
Cath: 1.10.45.10; 3.30.43.10; 3.30.465.10; 3.40.462.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.1.3.38
BRENDA Enzyme Link: BRENDA 1.1.3.38
KEGG Enzyme Link: KEGG1.1.3.38
BioCyc Enzyme Link: BioCyc 1.1.3.38
ExPASy Enzyme Link: ExPASy1.1.3.38
EC2PDB Enzyme Link: EC2PDB 1.1.3.38
ExplorEnz Enzyme Link: ExplorEnz 1.1.3.38
PRIAM enzyme-specific profiles Link: PRIAM 1.1.3.38
IntEnz Enzyme Link: IntEnz 1.1.3.38
MEDLINE Enzyme Link: MEDLINE 1.1.3.38
MSA:

1.1.3.38;

Phylogenetic Tree:

1.1.3.38;

Uniprot:
M-CSA:
RHEA:10036 4-hydroxy-3-methoxy-benzenemethanol + O2 = 4-hydroxy-3-methoxybenzaldehyde + H2O2
RULE(radius=1) [*:1]-[CH2;+0:2]-[OH;+0:3].[O;H0;+0:4]=[O;H0;+0:5]>>[*:1]-[CH;+0:2]=[O;H0;+0:3].[OH;+0:4]-[OH;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity.Mattevi A, Fraaije MW, Mozzarelli A, Olivi L, Coda A, van Berkel WJ1997 Jul 159261083
Substrate specificity of flavin-dependent vanillyl-alcohol oxidase from Penicillium simplicissimum. Evidence for the production of 4-hydroxycinnamyl alcohols from 4-allylphenols.Fraaije MW, Veeger C, van Berkel WJ1995 Nov 158529652
Purification and characterization of vanillyl-alcohol oxidase from Penicillium simplicissimum. A novel aromatic alcohol oxidase containing covalently bound FAD.de Jong E, van Berkel WJ, van der Zwan RP, de Bont JA1992 Sep 151396672