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Literature summary for 1.14.13.39 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)

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

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
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
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 Staphylococcus aureus
-
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 Bacillus subtilis
-
2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Staphylococcus aureus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant bNOS by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration Staphylococcus aureus
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
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
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
-
Staphylococcus aureus 2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2
-
Bacillus subtilis 2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
?
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
-
?
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
-
?
Nomega-hydroxy-L-arginine + NADPH + H+ + O2 second half reaction via intermediate Nomega-hydroxy-L-arginine Bacillus subtilis citrulline + nitric oxide + NADP+ + H2O
-
?
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

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

Cofactor

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