Cloned (Comment) | Organism |
---|---|
DNA and amino acid sequence determination and analysis, functional expression of the C-terminally His6-tagged soluble enzyme in Escherichia coli strain BL21 (DE3), sequence alignment and comparative modeling | Bacillus anthracis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
imidazole | the enzyme forms a sixcoordinate low-spin complex with inhibitor imidazole, interaction analysis | Bacillus anthracis | |
NG-methyl arginine | specific inhibition | Bacillus anthracis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Iron | as heme iron in protoporphyrin IX /heme, hemesubstrate interactions and heme-transitions, overview | Bacillus anthracis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
43000 | - |
x * 43000, recombinant His6-tagged enzyme, SDS-PAGE | Bacillus anthracis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 L-arginine + 3 NADPH + 4 O2 + 3 H+ | Bacillus anthracis | - |
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O | - |
? | |
additional information | Bacillus anthracis | the enzyme is involved in a multi-turnover process that results in NO as a product, NO is important in various pathological and physiological processes, NO produced by Bacillus anthracis may also have a pivotal pathophysiological role in anthrax infection | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus anthracis | - |
pathogenic bacterium responsible for causing anthrax | - |
Purification (Comment) | Organism |
---|---|
recombinant His6-tagged soluble enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography | Bacillus anthracis |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O | the key structural features that are involved in the substrate and active site interaction are highly conserved, e.g. residues Pro214, Glu235, Trp234, Tyr237, Asn246, and Gln129, substrate binding structure and mechanism, overview | Bacillus anthracis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 L-arginine + 3 NADPH + 4 O2 + 3 H+ | - |
Bacillus anthracis | 2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O | - |
? | |
2 L-arginine + 3 NADPH + 4 O2 + 3 H+ | the enzyme forms a five-coordinate, high-spin complex with L-arginine and analogues, e.g. N-hydroxy-L-arginine | Bacillus anthracis | 2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O | - |
? | |
additional information | the enzyme is involved in a multi-turnover process that results in NO as a product, NO is important in various pathological and physiological processes, NO produced by Bacillus anthracis may also have a pivotal pathophysiological role in anthrax infection | Bacillus anthracis | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 43000, recombinant His6-tagged enzyme, SDS-PAGE | Bacillus anthracis |
More | bimodal enzyme, comprising of an N-terminal oxygenase domain that binds protoporphyrin IX /heme, 6R-tetrahydrobiopterin, and L-arginine, and a C-terminal reductase domain that binds FMN, FAD, and NADPH, the two domains are linked together by a calmodulin binding sequence | Bacillus anthracis |
Synonyms | Comment | Organism |
---|---|---|
nitric oxide synthase | - |
Bacillus anthracis |
nitric oxide synthase-like protein | - |
Bacillus anthracis |
NOS | - |
Bacillus anthracis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
(6R)-tetrahydrobiopterin | enzyme-bound | Bacillus anthracis | |
Calmodulin | enzyme-bound, the binding sequence links the two enzyme domains | Bacillus anthracis | |
FAD | enzyme-bound | Bacillus anthracis | |
FMN | enzyme-bound | Bacillus anthracis | |
NADPH | - |
Bacillus anthracis |