Nitronate monooxygenase

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
Nitronate monooxygenase
Identifiers
EC number1.13.12.16
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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.
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