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

Nitric-oxide synthase (NAD(P)H-dependent)
Identifiers
EC number 1.14.13.165
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Nitric-oxide synthase (NAD(P)H-dependent) (EC 1.14.13.165, 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 \rightleftharpoons 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 \rightleftharpoons 2 Nomega-hydroxy-L-arginine + 2 NAD(P)+ + 2 H2O
(1b) 2 Nomega-hydroxy-L-arginine + NAD(P)H + H+ + 2 O2 \rightleftharpoons 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, Z.Q., Lawson, R.J., Buddha, M.R., Wei, C.C., Crane, B.R., Munro, A.W. and Stuehr, D.J. (2007). "Bacterial flavodoxins support nitric oxide production by Bacillus subtilis nitric-oxide synthase". J. Biol. Chem. 282 (4): 2196–2202. doi:10.1074/jbc.M608206200. PMID 17127770.
  2. ↑ Gusarov, I., Starodubtseva, M., Wang, Z.Q., McQuade, L., Lippard, S.J., Stuehr, D.J. and Nudler, E. (2008). "Bacterial nitric-oxide synthases operate without a dedicated redox partner". J. Biol. Chem. 283: 13140–13147. doi:10.1074/jbc.M710178200. PMC 2442334. PMID 18316370.
  3. ↑ Agapie, T., Suseno, S., Woodward, J.J., Stoll, S., Britt, R.D. and Marletta, M.A. (2009). "NO formation by a catalytically self-sufficient bacterial nitric oxide synthase from Sorangium cellulosum". Proc. Natl. Acad. Sci. USA 106 (38): 16221–16226. doi:10.1073/pnas.0908443106. PMC 2752531. PMID 19805284.

External links

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