From Wikipedia, the free encyclopedia
Nitric-oxide synthase (NAD(P)H-dependent)
Identifiers
EC no. 1.14.14.47
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

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 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 2 N-omega-hydroxy-L-arginine + 2 NAD(P)+ + 2 H2O
(1b) 2 N-omega-hydroxy-L-arginine + NAD(P)H + H+ + 2 O2 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. ^ Wang ZQ, Lawson RJ, Buddha MR, Wei CC, Crane BR, Munro AW, Stuehr DJ (January 2007). "Bacterial flavodoxins support nitric oxide production by Bacillus subtilis nitric-oxide synthase". The Journal of Biological Chemistry. 282 (4): 2196–202. doi: 10.1074/jbc.M608206200. PMID  17127770.
  2. ^ Gusarov I, Starodubtseva M, Wang ZQ, McQuade L, Lippard SJ, Stuehr DJ, Nudler E (May 2008). "Bacterial nitric-oxide synthases operate without a dedicated redox partner". The Journal of Biological Chemistry. 283 (19): 13140–7. doi: 10.1074/jbc.M710178200. PMC  2442334. PMID  18316370.
  3. ^ Agapie T, Suseno S, Woodward JJ, Stoll S, Britt RD, Marletta MA (September 2009). "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. doi: 10.1073/pnas.0908443106. PMC  2752531. PMID  19805284.
From Wikipedia, the free encyclopedia
Nitric-oxide synthase (NAD(P)H-dependent)
Identifiers
EC no. 1.14.14.47
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

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 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 2 N-omega-hydroxy-L-arginine + 2 NAD(P)+ + 2 H2O
(1b) 2 N-omega-hydroxy-L-arginine + NAD(P)H + H+ + 2 O2 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. ^ Wang ZQ, Lawson RJ, Buddha MR, Wei CC, Crane BR, Munro AW, Stuehr DJ (January 2007). "Bacterial flavodoxins support nitric oxide production by Bacillus subtilis nitric-oxide synthase". The Journal of Biological Chemistry. 282 (4): 2196–202. doi: 10.1074/jbc.M608206200. PMID  17127770.
  2. ^ Gusarov I, Starodubtseva M, Wang ZQ, McQuade L, Lippard SJ, Stuehr DJ, Nudler E (May 2008). "Bacterial nitric-oxide synthases operate without a dedicated redox partner". The Journal of Biological Chemistry. 283 (19): 13140–7. doi: 10.1074/jbc.M710178200. PMC  2442334. PMID  18316370.
  3. ^ Agapie T, Suseno S, Woodward JJ, Stoll S, Britt RD, Marletta MA (September 2009). "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. doi: 10.1073/pnas.0908443106. PMC  2752531. PMID  19805284.

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