4-Nitrocatechol 4-monooxygenase

4-nitrocatechol 4-monooxygenase
Identifiers
EC no.	1.14.13.166
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

4-nitrocatechol 4-monooxygenase (EC 1.14.13.166) is an enzyme with systematic name 4-nitrocatechol,NAD(P)H:oxygen 4-oxidoreductase (4-hydroxylating, nitrite-forming).^[1][2][3] This enzyme catalyses the following chemical reaction:

4-nitrocatechol + NAD(P)H + H⁺ + O₂ ${\displaystyle \rightleftharpoons }$ 2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H₂O

4-nitrocatechol 4-monooxygenase contains flavin adenine dinucleotide (FAD).^{[citation needed]}

References

1. Kadiyala V, Spain JC (July 1998). "A two-component monooxygenase catalyzes both the hydroxylation of p-nitrophenol and the oxidative release of nitrite from 4-nitrocatechol in Bacillus sphaericus JS905". Applied and Environmental Microbiology. 64 (7): 2479–84. PMC 106414. PMID 9647818.
2. Kitagawa W, Kimura N, Kamagata Y (August 2004). "A novel p-nitrophenol degradation gene cluster from a gram-positive bacterium, Rhodococcus opacus SAO101". Journal of Bacteriology. 186 (15): 4894–902. doi:10.1128/JB.186.15.4894-4902.2004. PMC 451640. PMID 15262926.
3. Zhang JJ, Liu H, Xiao Y, Zhang XE, Zhou NY (April 2009). "Identification and characterization of catabolic para-nitrophenol 4-monooxygenase and para-benzoquinone reductase from Pseudomonas sp. strain WBC-3". Journal of Bacteriology. 191 (8): 2703–10. doi:10.1128/JB.01566-08. PMC 2668391. PMID 19218392.

External links

• 4-nitrocatechol+4-monooxygenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)