| 4-hydroxybenzoate 3-monooxygenase [NAD(P)H] | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.33 | ||||||||
| CAS no. | 95471-33-3 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a 4-hydroxybenzoate 3-monooxygenase [NAD(P)H] (EC 1.14.13.33) is an enzyme that catalyzes the chemical reaction
- 4-hydroxybenzoate + NAD(P)H + H+ + O2 3,4-dihydroxybenzoate + NAD(P)+ + H2O
The 5 substrates of this enzyme are 4-hydroxybenzoate, NADH, NADPH, H+, and O2, whereas its 4 products are 3,4-dihydroxybenzoate, NAD+, NADP+, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is 4-hydroxybenzoate,NAD(P)H:oxygen oxidoreductase (3-hydroxylating). Other names in common use include 4-hydroxybenzoate 3-monooxygenase (reduced nicotinamide adenine, dinucleotide (phosphate)), 4-hydroxybenzoate-3-hydroxylase, and 4-hydroxybenzoate 3-hydroxylase. This enzyme participates in benzoate degradation via hydroxylation and 2,4-dichlorobenzoate degradation. It employs one cofactor, FAD.
References[edit]
- Fujii T, Kaneda T (1985). "Purification and properties of NADH/NADPH-dependent p-hydroxybenzoate hydroxylase from Corynebacterium cyclohexanicum". Eur. J. Biochem. 147 (1): 97–104. doi:10.1111/j.1432-1033.1985.tb08724.x. PMID 3971979.
- Seibold B, Matthes M, Eppink MH, Lingens F, Van Berkel WJ, Muller R (1996). "4-Hydroxybenzoate hydroxylase from Pseudomonas sp. CBS3 Purification, characterization, gene cloning, sequence analysis and assignment of structural features determining the coenzyme specificity". Eur. J. Biochem. 239 (2): 469–78. doi:10.1111/j.1432-1033.1996.0469u.x. PMID 8706756.
