Biology:4-Nitrocatechol 4-monooxygenase
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Short description: Class of enzymes
4-nitrocatechol 4-monooxygenase | |||||||||
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Identifiers | |||||||||
EC number | 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] 2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
4-nitrocatechol 4-monooxygenase contains flavin adenine dinucleotide (FAD).[citation needed]
References
- ↑ "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. July 1998. PMID 9647818.
- ↑ "A novel p-nitrophenol degradation gene cluster from a gram-positive bacterium, Rhodococcus opacus SAO101". Journal of Bacteriology 186 (15): 4894–902. August 2004. doi:10.1128/JB.186.15.4894-4902.2004. PMID 15262926.
- ↑ "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. April 2009. doi:10.1128/JB.01566-08. PMID 19218392.
External links
- 4-nitrocatechol+4-monooxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)
![]() | Original source: https://en.wikipedia.org/wiki/4-Nitrocatechol 4-monooxygenase.
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