In enzymology, a 4-nitrophenol 2-monooxygenase (EC 1.14.13.29) is an enzyme that catalyzes the chemical reaction
4-nitrophenol 2-monooxygenase | |||||||||
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Identifiers | |||||||||
EC no. | 1.14.13.29 | ||||||||
CAS no. | 91116-87-9 | ||||||||
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 | ||||||||
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- 4-nitrophenol + NADH + H+ + O2 4-nitrocatechol + NAD+ + H2O
The 4 substrates of this enzyme are 4-nitrophenol, NADH, H+, and O2, whereas its 3 products are 4-nitrocatechol, NAD+, 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-nitrophenol,NADH:oxygen oxidoreductase (2-hydroxylating). Other names in common use include 4-nitrophenol hydroxylase, and 4-nitrophenol-2-hydroxylase. This enzyme participates in gamma-hexachlorocyclohexane degradation. It employs one cofactor, FAD.
References
edit- Mitra D, Vaidyanathan CS (1984). "A new 4-nitrophenol 2-hydroxylase from a Nocardia sp". Biochem. Int. 8 (5): 609–15. PMID 6477623.