Biology:Nitronate monooxygenase
From HandWiki
| 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 [math]\displaystyle{ \rightleftharpoons }[/math] 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
- ↑ "Involvement of a flavosemiquinone in the enzymatic oxidation of nitroalkanes catalyzed by 2-nitropropane dioxygenase". The Journal of Biological Chemistry 280 (7): 5195–204. February 2005. doi:10.1074/jbc.M411249200. PMID 15582992.
- ↑ "Crystal structure of 2-nitropropane dioxygenase complexed with FMN and substrate. Identification of the catalytic base". The Journal of Biological Chemistry 281 (27): 18660–7. July 2006. doi:10.1074/jbc.M601658200. PMID 16682407.
- ↑ "Nitronate monooxygenase, a model for anionic flavin semiquinone intermediates in oxidative catalysis". Archives of Biochemistry and Biophysics 493 (1): 53–61. January 2010. doi:10.1016/j.abb.2009.06.018. PMID 19577534.
- ↑ "Kinetic evidence for an anion binding pocket in the active site of nitronate monooxygenase". Bioorganic Chemistry 37 (5): 167–72. October 2009. 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)
 |  |
