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Literature summary 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)

EC Number Cloned (Comment) Organism
1.14.13.39 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

EC Number Inhibitors Comment Organism Structure
1.14.13.39 imidazole the enzyme forms a sixcoordinate low-spin complex with inhibitor imidazole, interaction analysis Bacillus anthracis
1.14.13.39 NG-methyl arginine specific inhibition Bacillus anthracis

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.13.39 43000
-
 x * 43000, recombinant His6-tagged enzyme, SDS-PAGE Bacillus anthracis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.39 2 L-arginine + 3 NADPH + 4 O2 + 3 H+ Bacillus anthracis
-
 2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
 ?
1.14.13.39 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

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

Purification (Commentary)

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

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.13.39 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
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.39 2 L-arginine + 3 NADPH + 4 O2 + 3 H+
-
 Bacillus anthracis 2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
 ?
1.14.13.39 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
-
 ?
1.14.13.39 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

EC Number Subunits Comment Organism
1.14.13.39 ? x * 43000, recombinant His6-tagged enzyme, SDS-PAGE Bacillus anthracis
1.14.13.39 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

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.39 (6R)-tetrahydrobiopterin enzyme-bound Bacillus anthracis
1.14.13.39 Calmodulin enzyme-bound, the binding sequence links the two enzyme domains Bacillus anthracis
1.14.13.39 FAD enzyme-bound Bacillus anthracis
1.14.13.39 FMN enzyme-bound Bacillus anthracis
1.14.13.39 NADPH
-
 Bacillus anthracis