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.
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 |
|