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Literature summary for 1.14.14.47 extracted from

  • Agapie, T.; Suseno, S.; Woodward, J.; Stoll, S.; Britt, R.; Marletta, M.
    NO formation by a catalytically self-sufficient bacterial nitric oxide synthase from Sorangium cellulosum (2009), Proc. Natl. Acad. Sci. USA, 106, 16221-16226.
    View publication on PubMedView publication on EuropePMC
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Metals/Ions

Metals/Ions Comment Organism Structure
Iron the enzyme's reductase domain utilizes a 2Fe2S cluster for electron transfer Sorangium cellulosum

Organism

Organism UniProt Comment Textmining
Sorangium cellulosum
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 L-arginine + 3 reduced flavodoxin + 4 O2 tetrahydrobiopterin or tetrahydrofolate may act as redox partners Sorangium cellulosum 2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O overall reaction ?

Subunits

Subunits Comment Organism
More enzyme contains a catalytic oxygenase domain with a fused reductase domain. The reductase domain utilizes a 2Fe2S cluster for electron transfer Sorangium cellulosum

Cofactor

Cofactor Comment Organism Structure
iron-sulfur centre the enzyme's reductase domain utilizes a 2Fe2S cluster for electron transfer Sorangium cellulosum
NADH small preference for NADH over NADPH Sorangium cellulosum
NADPH small preference for NADH over NADPH Sorangium cellulosum
tetrahydrobiopterin or tetrahydrofolate Sorangium cellulosum
tetrahydrofolate or tetrahydrobiopterin Sorangium cellulosum