ENZYME entry: EC 1.13.12.16

Accepted Name
Nitronate monooxygenase.
Alternative Name(s)
2-nitropropane dioxygenase.
2-NPD.
Nitroalkane oxidase.
NMO.
Reaction catalysed
Ethylnitronate + O(2) <=> acetaldehyde + nitrite + other products
Cofactor(s)
FMN.
Comment(s)
  • Previously classified as EC 1.13.11.32, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms.
  • The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor.
  • Neither hydrogen peroxide nor superoxide were detected during enzyme turnover.
  • Active toward linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, toward propyl-2-nitronate.
  • The enzyme from N.crassa can also utilize neutral nitroalkanes, but with lower activity.
  • Formerly EC 1.13.11.32.
Cross-references
BRENDA1.13.12.16
EC2PDB1.13.12.16
ExplorEnz1.13.12.16
PRIAM enzyme-specific profiles1.13.12.16
KEGG Ligand Database for Enzyme Nomenclature1.13.12.16
IUBMB Enzyme Nomenclature1.13.12.16
IntEnz1.13.12.16
MEDLINEFind literature relating to 1.13.12.16
MetaCyc1.13.12.16
UniProtKB/Swiss-Prot
P47177, 2NDP_YEAST;  O05413, 2NPD_BACSU;  Q12723, 2NPD_CYBMR;  
Q01284, 2NPD_NEUCR;  Q9I4V0, 2NPD_PSEAE;  A6U025, 2NPD_STAA2;  
Q2FIF3, 2NPD_STAA3;  Q2FZX9, 2NPD_STAA8;  A5IR97, 2NPD_STAA9;  
Q5HHG4, 2NPD_STAAC;  A6QFD2, 2NPD_STAAE;  Q99VF6, 2NPD_STAAN;  
Q6GIG7, 2NPD_STAAR;  Q6GB05, 2NPD_STAAS;  A8Z1H7, 2NPD_STAAT;  
Q8NXG7, 2NPD_STAAW;  Q4L4T4, 2NPD_STAHJ;  Q49W60, 2NPD_STAS1;  

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