4-hydroxybenzoate 3-monooxygenase
| 4-hydroxybenzoate 3-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.2 | ||||||||
| CAS no. | 9059-23-8 | ||||||||
| 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 (EC 1.14.13.2) is an enzyme that catalyzes the chemical reaction
- 4-hydroxybenzoate + NADPH + H+ + O2 protocatechuate + NADP+ + H2O
The 4 substrates of this enzyme are 4-hydroxybenzoate, NADPH, H+, and O2, whereas its 3 products are protocatechuate, NADP+, and H2O.
This enzyme participates in benzoate degradation via hydroxylation. It employs one cofactor, FAD.
Nomenclature
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,NADPH:oxygen oxidoreductase (3-hydroxylating). Other names in common use include:
- p-hydroxybenzoate hydrolyase,
- p-hydroxybenzoate hydroxylase,
- 4-hydroxybenzoate 3-hydroxylase,
- 4-hydroxybenzoate monooxygenase,
- 4-hydroxybenzoic hydroxylase,
- p-hydroxybenzoate-3-hydroxylase,
- p-hydroxybenzoic acid hydrolase,
- p-hydroxybenzoic acid hydroxylase, and
- p-hydroxybenzoic hydroxylase.
References
Further reading
- Hosokawa K, Stanier RY (May 1966). "Crystallization and properties of p-hydroxybenzoate hydroxylase from Pseudomonas putida". The Journal of Biological Chemistry. 241 (10): 2453–60. PMID 4380381.
- Howell LG, Spector T, Massey V (July 1972). "Purification and properties of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens". The Journal of Biological Chemistry. 247 (13): 4340–50. PMID 4402514.
- Spector T, Massey V (July 1972). "Studies on the effector specificity of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens". The Journal of Biological Chemistry. 247 (14): 4679–87. PMID 4402938.
- Spector T, Massey V (September 1972). "p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Evidence for an oxygenated flavin intermediate". The Journal of Biological Chemistry. 247 (17): 5632–6. PMID 4403446.
- Spector T, Massey V (November 1972). "p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Reactivity with oxygen". The Journal of Biological Chemistry. 247 (22): 7123–7. PMID 4404745.
- Seibold B, Matthes M, Eppink MH, Lingens F, Van Berkel WJ, Müller R (July 1996). "4-Hydroxybenzoate hydroxylase from Pseudomonas sp. CBS3. Purification, characterization, gene cloning, sequence analysis and assignment of structural features determining the coenzyme specificity". European Journal of Biochemistry. 239 (2): 469–78. doi:10.1111/j.1432-1033.1996.0469u.x. PMID 8706756.