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Literature summary for 1.14.13.39 extracted from

  • Midha, S.; Mishra, R.; Aziz, M.A.; Sharma, M.; Mishra, A.; Khandelwal, P.; Bhatnagar, R.
    Cloning, expression, and characterization of recombinant nitric oxide synthase-like protein from Bacillus anthracis (2005), Biochem. Biophys. Res. Commun., 336, 346-356.
    View publication on PubMed

Cloned(Commentary)

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

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

Metals/Ions Comment Organism Structure
Iron as heme iron in protoporphyrin IX /heme, heme–substrate interactions and heme-transitions, overview Bacillus anthracis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
x * 43000, recombinant His6-tagged enzyme, SDS-PAGE Bacillus anthracis

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Bacillus anthracis
-
pathogenic bacterium responsible for causing anthrax
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged soluble enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography Bacillus anthracis

Reaction

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 and Products (Substrate)

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

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

Synonyms Comment Organism
nitric oxide synthase
-
Bacillus anthracis
nitric oxide synthase-like protein
-
Bacillus anthracis
NOS
-
Bacillus anthracis

Cofactor

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