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
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 $\rightleftharpoons$ 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. and 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.
2. 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. and 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.
3. Gadda, G. and 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.
4. Francis, K. and 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)