In enzymology, a phenol 2-monooxygenase (EC 1.14.13.7) is an enzyme that catalyzes the chemical reaction
| phenol 2-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.13.7 | ||||||||
| CAS no. | 37256-84-1 | ||||||||
| 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 | ||||||||
| |||||||||
- phenol + NADPH + H+ + O2 catechol + NADP+ + H2O
The 4 substrates of this enzyme are phenol, NADPH, H+, and O2, whereas its 3 products are catechol, 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 phenol,NADPH:oxygen oxidoreductase (2-hydroxylating). Other names in common use include phenol hydroxylase, and phenol o-hydroxylase. This enzyme participates in 3 metabolic pathways: gamma-hexachlorocyclohexane degradation, toluene and xylene degradation, and naphthalene and anthracene degradation. It employs one cofactor, FAD.
Structural studies
editAs of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1FOH, 1HQI, and 1PN0.
References
edit- NAKAGAWA H, TAKEDA Y (1962). "Phenol hydroxylase". Biochim. Biophys. Acta. 62 (2): 423–6. doi:10.1016/0006-3002(62)90275-5. PMID 14478080.
- Neujahr HY, Gaal A (1973). "Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum". Eur. J. Biochem. 35 (2): 386–400. doi:10.1111/j.1432-1033.1973.tb02851.x. PMID 4146224.
- Neujahr HY, Gaal A (1975). "Phenol hydroxylase from yeast. Sulfhydryl groups in phenol hydroxylase from Trichosporon cutaneum". Eur. J. Biochem. 58 (2): 351–7. doi:10.1111/j.1432-1033.1975.tb02381.x. PMID 810352.
