Nitronate monooxygenase

Nitronate monooxygenase
Identifiers
EC no.	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
Search PMC articles PubMed articles NCBI proteins

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${\displaystyle \rightleftharpoons }$ 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

1. Francis K, Russell B, Gadda G (February 2005). "Involvement of a flavosemiquinone in the enzymatic oxidation of nitroalkanes catalyzed by 2-nitropropane dioxygenase". The Journal of Biological Chemistry. 280 (7): 5195–204. doi: 10.1074/jbc.M411249200 . PMID   15582992.
2. Ha JY, Min JY, Lee SK, Kim HS, Kim DJ, Kim KH, Lee HH, Kim HK, Yoon HJ, Suh SW (July 2006). "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. doi: 10.1074/jbc.M601658200 . PMID   16682407.
3. Gadda G, Francis K (January 2010). "Nitronate monooxygenase, a model for anionic flavin semiquinone intermediates in oxidative catalysis". Archives of Biochemistry and Biophysics. 493 (1): 53–61. doi:10.1016/j.abb.2009.06.018. PMID   19577534.
4. Francis K, Gadda G (October 2009). "Kinetic evidence for an anion binding pocket in the active site of nitronate monooxygenase". Bioorganic Chemistry. 37 (5): 167–72. doi:10.1016/j.bioorg.2009.07.005. PMID   19683782.

External links

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