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Literature summary extracted from

  • Adak, S.; Aulak, K.S.; Stuehr, D.J.
    Direct evidence for nitric oxide production by a nitric-oxide synthase-like protein from Bacillus subtilis (2002), J. Biol. Chem., 277, 16167-16171.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.14.47 0.0001
-
 tetrahydrobiopterin pH 7.6, 25°C Bacillus subtilis
1.14.14.47 0.0004
-
 tetrahydrofolate pH 7.6, 25°C Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.47 Bacillus subtilis O34453
-
-
1.14.14.47 Bacillus subtilis 168 O34453
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.47 2 L-arginine + 2 tetrahydrobiopterin + 2 O2
-
 Bacillus subtilis 2 Nomega-hydroxy-L-arginine + 2 oxidized tetrahydrobiopterin + 2 H2O
-
 ?
1.14.14.47 2 L-arginine + 2 tetrahydrobiopterin + 2 O2
-
 Bacillus subtilis 168 2 Nomega-hydroxy-L-arginine + 2 oxidized tetrahydrobiopterin + 2 H2O
-
 ?
1.14.14.47 2 L-arginine + 3 tetrahydrobiopterin + 4 O2
-
 Bacillus subtilis 2 L-citrulline + 2 nitric oxide + 3 oxidized tetrahydrobiopterin + 4 H2O overall reaction ?
1.14.14.47 2 L-arginine + 3 tetrahydrobiopterin + 4 O2
-
 Bacillus subtilis 168 2 L-citrulline + 2 nitric oxide + 3 oxidized tetrahydrobiopterin + 4 H2O overall reaction ?
1.14.14.47 2 L-arginine + 3 tetrahydrofolate + 4 O2
-
 Bacillus subtilis 2 L-citrulline + 2 nitric oxide + 3 oxidized tetrahydrofolate + 4 H2O overall reaction ?
1.14.14.47 2 L-arginine + 3 tetrahydrofolate + 4 O2
-
 Bacillus subtilis 168 2 L-citrulline + 2 nitric oxide + 3 oxidized tetrahydrofolate + 4 H2O overall reaction ?
1.14.14.47 2 Nomega-hydroxy-L-arginine + tetrahydrobiopterin + 2 O2
-
 Bacillus subtilis 2 L-citrulline + 2 nitric oxide + oxidized tetrahydrobiopterin + 2 H2O
-
 ?
1.14.14.47 2 Nomega-hydroxy-L-arginine + tetrahydrobiopterin + 2 O2
-
 Bacillus subtilis 168 2 L-citrulline + 2 nitric oxide + oxidized tetrahydrobiopterin + 2 H2O
-
 ?
1.14.14.47 additional information ferrous bsNOS reacts with O2 to form a transient heme Fe(II)O2 species in the presence of either Arg or the reaction intermediate N-hydroxy-L-arginine. Disappearance of the Fe(II)O2 species is kinetically and quantitatively coupled to formation of a transient heme Fe(III)NO product, which then dissociates to form ferric NOS. NO formation requires a bound tetrahydropteridine, and the kinetic effects of this cofactor are consistent with it donating an electron to the Fe(II)O2 intermediate during the reaction. Dissociation of the heme Fe(III)NO product is much slower than in mammalian NOS Bacillus subtilis ?
-
 ?
1.14.14.47 additional information ferrous bsNOS reacts with O2 to form a transient heme Fe(II)O2 species in the presence of either Arg or the reaction intermediate N-hydroxy-L-arginine. Disappearance of the Fe(II)O2 species is kinetically and quantitatively coupled to formation of a transient heme Fe(III)NO product, which then dissociates to form ferric NOS. NO formation requires a bound tetrahydropteridine, and the kinetic effects of this cofactor are consistent with it donating an electron to the Fe(II)O2 intermediate during the reaction. Dissociation of the heme Fe(III)NO product is much slower than in mammalian NOS Bacillus subtilis 168 ?
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.14.47 0.183
-
 tetrahydrobiopterin pH 7.6, 25°C Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.47 heme
-
 Bacillus subtilis
1.14.14.47 tetrahydrobiopterin NO formation requires a bound tetrahydropteridine, and the kinetic effects are consistent with it donating an electron to the Fe(II)O2 intermediate during the reaction Bacillus subtilis