| Entry |
|
| Name |
vanillyl-alcohol oxidase;
4-hydroxy-2-methoxybenzyl alcohol oxidase |
| Class |
Oxidoreductases;
Acting on the CH-OH group of donors;
With oxygen as acceptor
 |
| Sysname |
vanillyl alcohol:oxygen oxidoreductase |
| Reaction(IUBMB) |
vanillyl alcohol + O2 = vanillin + H2O2 [RN:R02877] |
| Reaction(KEGG) |
R02877
 |
| Substrate |
vanillyl alcohol [CPD:C06317];
O2 [CPD:C00007] |
| Product |
vanillin [CPD:C00755];
H2O2 [CPD:C00027] |
| Cofactor |
FAD [CPD:C00016] |
| Comment |
Vanillyl-alcohol oxidase from Penicillium simplicissimum contains
covalently bound FAD. It converts a wide range of 4-hydroxybenzyl
alcohols and 4-hydroxybenzylamines into the corresponding aldehydes.
The allyl group of 4-allylphenols is also converted into the
-CH=CH-CH2OH group. |
| Pathway |
PATH: ec00623 2,4-Dichlorobenzoate degradation |
| Structures |
PDB: 1DZN 1E0Y 1E8G |
Reference Authors Title
Journal Organism
|
1 [PMID:1396672]
de Jong E, van Berkel WJ, van der Zwan RP, de Bont JA.
Purification and characterization of vanillyl-alcohol oxidase from
Penicillium simplicissimum. A novel aromatic alcohol oxidase
containing covalently bound FAD.
Eur. J. Biochem. 208 (1992) 651-7.
Penicillium simplicissimum |
Reference Authors Title
Journal Organism
|
2 [PMID:8529652]
Fraaije MW, Veeger C, van Berkel WJ.
Substrate specificity of flavin-dependent vanillyl-alcohol oxidase
from Penicillium simplicissimum. Evidence for the production of
4-hydroxycinnamyl alcohols from 4-allylphenols.
Eur. J. Biochem. 234 (1995) 271-7.
Penicillium simplicissimum |
| Other DBs |
ExplorEnz - The Enzyme Database: 1.1.3.38
IUBMB Enzyme Nomenclature: 1.1.3.38
ExPASy - ENZYME nomenclature database: 1.1.3.38
UM-BBD (Biocatalysis/Biodegradation Database): 1.1.3.38
BRENDA, the Enzyme Database: 1.1.3.38
CAS: 143929-24-2 |