Vanillate monooxygenase
| Vanillate monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.82 | ||||||||
| CAS no. | 39307-11-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Vanillate monooxygenase (EC 1.14.13.82) is an enzyme that catalyzes the chemical reaction
The four substrates of this enzyme are vanillic acid, reduced nicotinamide adenine dinucleotide (NADH), oxygen, and a proton. Its products are protocatechuic acid, oxidised NAD+, water, and formaldehyde.[1][2]
This enzyme is an oxidoreductase, acting on paired donors, with molecular oxygen as oxidant and incorporating one of its atoms. The systematic name of this enzyme class is vanillate:oxygen oxidoreductase (demethylating). Other names in common use include 4-hydroxy-3-methoxybenzoate demethylase, and vanillate demethylase. This enzyme participates in vanillin degradation in Pseudomonas bacteria.[3]
References
- ^ Enzyme 1.14.13.82 at KEGG Pathway Database.
- ^ Brunel F, Davison J (1988). "Cloning and sequencing of Pseudomonas genes encoding vanillate demethylase". J. Bacteriol. 170 (10): 4924–4930. doi:10.1128/jb.170.10.4924-4930.1988. PMC 211539. PMID 3170489.
- ^ Priefert H, Rabenhorst J, Steinbüchel A (1997). "Molecular characterization of genes of Pseudomonas sp. strain HR199 involved in bioconversion of vanillin to protocatechuate". J. Bacteriol. 179 (8): 2595–2607. doi:10.1128/jb.179.8.2595-2607.1997. PMC 179009. PMID 9098058.