Cloned (Comment) | Organism |
---|---|
- |
Bacillus subtilis |
Protein Variants | Comment | Organism |
---|---|---|
I224V | little effect on binding of L-arginie, tetrahydrobiopterin or in electronic properties | Bacillus subtilis |
I224V | mutation does not greatly alter binding of Arg, (6R)-tetrahydrobiopterin, or alter the electronic properties of the heme or various heme-ligand complexes. I224V displays three heme transitions involving four species as typically occurs in wild-type NOS, the beginning ferrous enzyme, a ferrous-dioxy (FeIIO2) intermediate, FeIIINO, and an ending ferric enzyme. The rate of each transition is increased relative to wild-type, with FeIIINO dissociation being 3.6 times faster | Bacillus subtilis |
V346I | slower NO-binding and dissociation than wild-type | Mus musculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
Bacillus subtilis | O34453 | - |
- |
Bacillus subtilis 168 | O34453 | - |
- |
Mus musculus | P29477 | inducible oxygenase domain | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O | analysis of transition states via stopped-flow spectroscopy | Bacillus subtilis | |
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O | analysis of transition states via stopped-flow spectroscopy | Mus musculus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
N-hydroxy-L-arginine + NADPH + O2 | - |
Bacillus subtilis | ? + NO + NADP+ | - |
? | |
N-hydroxy-L-arginine + NADPH + O2 | - |
Mus musculus | ? + NO + NADP+ | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
5,6,7,8-tetrahydro-L-biopterin | - |
Bacillus subtilis | |
5,6,7,8-tetrahydro-L-biopterin | - |
Mus musculus | |
NADPH | - |
Bacillus subtilis | |
NADPH | - |
Mus musculus |