Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.47 Sorangium cellulosum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.47 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

EC Number Subunits Comment Organism
1.14.14.47 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

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