Nitronate monooxygenase
| Nitronate monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.13.12.16 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Nitronate monooxygenase (EC 1.13.12.16, NMO) is an enzyme with systematic name nitronate:oxygen 2-oxidoreductase (nitrite-forming).[1][2][3][4] This enzyme catalyses the following chemical reaction
- ethylnitronate + O2 acetaldehyde + nitrite + other products
The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii contain non-covalently bound FMN as the cofactor.
References
- ↑ Francis, K.; Russell, B.; Gadda, G. (2005). "Involvement of a flavosemiquinone in the enzymatic oxidation of nitroalkanes catalyzed by 2-nitropropane dioxygenase". J. Biol. Chem. 280: 5195–5204. doi:10.1074/jbc.M411249200. PMID 15582992.
- ↑ Ha, J.Y.; Min, J.Y.; Lee, S.K.; Kim, H.S.; Kim do, J.; Kim, K.H.; Lee, H.H.; Kim, H.K.; Yoon, H.J.; Suh, S.W. (2006). "Crystal structure of 2-nitropropane dioxygenase complexed with FMN and substrate. Identification of the catalytic base". J. Biol. Chem. 281: 18660–18667. doi:10.1074/jbc.M601658200. PMID 16682407.
- ↑ Gadda, G.; Francis, K. (2010). "Nitronate monooxygenase, a model for anionic flavin semiquinone intermediates in oxidative catalysis". Arch. Biochem. Biophys. 493 (1): 53–61. doi:10.1016/j.abb.2009.06.018. PMID 19577534.
- ↑ Francis, K.; Gadda, G. (2009). "Kinetic evidence for an anion binding pocket in the active site of nitronate monooxygenase". Bioorg. Chem. 37 (5): 167–172. doi:10.1016/j.bioorg.2009.07.005. PMID 19683782.
External links
- Nitronate monooxygenase at the US National Library of Medicine Medical Subject Headings (MeSH)
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