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Literature summary extracted from

  • Chartier, F.J.; Couture, M.
    Interactions between substrates and the haem-bound nitric oxide of ferric and ferrous bacterial nitric oxide synthases (2007), Biochem. J., 401, 235-245.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.39 overexpression of His6-tagged bNOS in Escherichia coli strain BL21(DE3) Bacillus subtilis
1.14.13.39 recombinant expression of bNOS Staphylococcus aureus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.39 additional information
-
 additional information kinetics of NO and substrate binding, recombinant enzyme Staphylococcus aureus
1.14.13.39 additional information
-
 additional information kinetics of NO and substrate binding, recombinant enzyme Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.13.39 Fe2+ a heme enzyme, spectral comparison of the FeIII-NO and FeII-NO complexes of the bacterial NOSs, FeIII-NO complexes lack change in Fe-N-O frequencies upon (6R) 5,6,7,8-tetrahydro-L-biopterin binding to bacterial NOSs, overview. In the FeIII-NO complexes, both L-arginine and NOHA induced the Fe-N-O bending mode at nearly the same frequency as a result of a steric interaction between the substrates and the heme-bound NO, while in FeII-NO complexes the the Fe-N-O bending mode is no observed Staphylococcus aureus
1.14.13.39 Fe2+ a heme enzyme, spectral comparison of the FeIII-NO and FeII-NO complexes of the bacterial NOSs, FeIII-NO complexes lack change in Fe-N-O frequencies upon (6R) 5,6,7,8-tetrahydro-L-biopterin binding to bacterial NOSs, overview. In the FeIII-NO complexes, both L-arginine and NOHA induced the Fe-N-O bending mode at nearly the same frequency as a result of a steric interaction between the substrates and the heme-bound NO, while in FeII-NO complexes the the Fe-N-O bending mode is no observed Bacillus subtilis

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 + 3 H+ + 4 O2 Staphylococcus aureus
-
 2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
 ?
1.14.13.39 2 L-arginine + 3 NADPH + 3 H+ + 4 O2 Bacillus subtilis
-
 2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.39 Bacillus subtilis
-
-
-
1.14.13.39 Staphylococcus aureus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.39 recombinant bNOS by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration Staphylococcus aureus
1.14.13.39 recombinant His6-tagged bNOS from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.39 2 L-arginine + 2 NADPH + 2 H+ + 2 O2 first half reaction via intermediate Nomega-hydroxy-L-arginine Staphylococcus aureus 2 Nomega-hydroxy-L-arginine + 2 NADP+ + 2 H2O
-
 ?
1.14.13.39 2 L-arginine + 2 NADPH + 2 H+ + 2 O2 first half reaction via intermediate Nomega-hydroxy-L-arginine Bacillus subtilis 2 Nomega-hydroxy-L-arginine + 2 NADP+ + 2 H2O
-
 ?
1.14.13.39 2 L-arginine + 3 NADPH + 3 H+ + 4 O2
-
 Staphylococcus aureus 2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
 ?
1.14.13.39 2 L-arginine + 3 NADPH + 3 H+ + 4 O2
-
 Bacillus subtilis 2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
 ?
1.14.13.39 2 L-arginine + 3 NADPH + 3 H+ + 4 O2 overall reaction, the interactions between heme-bound NO and the substrates are finely tuned by the geometry of the Fe-ligand structure, overview Staphylococcus aureus 2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
 ?
1.14.13.39 2 L-arginine + 3 NADPH + 3 H+ + 4 O2 overall reaction, the interactions between heme-bound NO and the substrates are finely tuned by the geometry of the Fe-ligand structure, overview Bacillus subtilis 2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
 ?
1.14.13.39 Nomega-hydroxy-L-arginine + NADPH + H+ + O2 second half reaction via intermediate Nomega-hydroxy-L-arginine Bacillus subtilis citrulline + nitric oxide + NADP+ + H2O
-
 ?
1.14.13.39 Nomega-hydroxy-L-arginine + NADPH + H+ + O2 second half reaction via intermediate Nomega-hydroxy-L-arginine, FeII and FeII-NO complexes bind Nomega-hydroxy-L-arginine, overview Staphylococcus aureus citrulline + nitric oxide + NADP+ + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.13.39 bacterial nitric oxide synthase
-
 Staphylococcus aureus
1.14.13.39 bacterial nitric oxide synthase
-
 Bacillus subtilis
1.14.13.39 bNOS
-
 Staphylococcus aureus
1.14.13.39 bNOS
-
 Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.39 heme b bound, quantitative determination Staphylococcus aureus
1.14.13.39 heme b bound, quantitative determination Bacillus subtilis
1.14.13.39 NADPH
-
 Staphylococcus aureus
1.14.13.39 NADPH
-
 Bacillus subtilis