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 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 | ||||||||
| |||||||||
- 4-nitrocatechol + NAD(P)H + H+ + O2 2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
4-nitrocatechol 4-monooxygenase contains flavin adenine dinucleotide (FAD).[citation needed]
References edit
- ^ 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.
- ^ 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.
- ^ 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 edit
- 4-nitrocatechol+4-monooxygenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
