Biology:Nitric-oxide synthase (NAD(P)H-dependent)

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Short description: Class of enzymes
Nitric-oxide synthase (NAD(P)H-dependent)
Identifiers
EC number1.14.14.47
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Nitric-oxide synthase (NAD(P)H-dependent) (EC 1.14.14.47, nitric oxide synthetase, NO synthase) is an enzyme with systematic name L-arginine,NAD(P)H:oxygen oxidoreductase (nitric-oxide-forming).[1][2][3] This enzyme catalyses the following chemical reaction

2 L-arginine + 3 NAD(P)H + 3 H+ + 4 O2 [math]\displaystyle{ \rightleftharpoons }[/math] 2 L-citrulline + 2 nitric oxide + 3 NAD(P)+ + 4 H2O (overall reaction)
(1a) 2 L-arginine + 2 NAD(P)H + 2 H+ + 2 O2 [math]\displaystyle{ \rightleftharpoons }[/math] 2 N-omega-hydroxy-L-arginine + 2 NAD(P)+ + 2 H2O
(1b) 2 N-omega-hydroxy-L-arginine + NAD(P)H + H+ + 2 O2 [math]\displaystyle{ \rightleftharpoons }[/math] 2 L-citrulline + 2 nitric oxide + NAD(P)+ + 2 H2O

Nitric-oxide synthase (NAD(P)H-dependent) binds heme (iron protoporphyrin IX) and tetrahydrobiopterin.

See also

References

  1. "Bacterial flavodoxins support nitric oxide production by Bacillus subtilis nitric-oxide synthase". The Journal of Biological Chemistry 282 (4): 2196–202. January 2007. doi:10.1074/jbc.M608206200. PMID 17127770. 
  2. "Bacterial nitric-oxide synthases operate without a dedicated redox partner". The Journal of Biological Chemistry 283 (19): 13140–7. May 2008. doi:10.1074/jbc.M710178200. PMID 18316370. 
  3. "NO formation by a catalytically self-sufficient bacterial nitric oxide synthase from Sorangium cellulosum". Proceedings of the National Academy of Sciences of the United States of America 106 (38): 16221–6. September 2009. doi:10.1073/pnas.0908443106. PMID 19805284. 

External links