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Literature summary extracted from

  • Wang, Z.; Lawson, R.J.; Buddha, M.R.; Wei, C.; Crane, B.R.; Munro, A.W.; Stuehr, D.J.
    Bacterial flavodoxins support nitric oxide production by Bacillus subtilis nitric-oxide synthase (2007), J. Biol. Chem., 282, 2196-2202.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.39 expression in Escherichia coli strain BL21(DE3) Bacillus subtilis

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 heme-NO complex formation in the stopped-flow reaction Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.13.39 Fe2+ a heme enzyme 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 Bacillus subtilis
-
 2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.39 Bacillus subtilis
-
-
-
1.14.14.47 Bacillus subtilis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.39 recombinant enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Bacillus subtilis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.14.13.39 additional information
-
 enzyme activities with different flavodoxins, overview 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 Bacillus subtilis 2 Nomega-hydroxy-L-arginine + 2 NADP+ + 2 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 Bacillus subtilis 2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
 ?
1.14.13.39 additional information the bacterial NOS enzymes have no attached flavoprotein domain to reduce their heme and so must rely on unknown bacterial proteins for electrons Bacillus subtilis ?
-
 ?
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
-
 ?
1.14.14.47 2 L-arginine + 3 reduced flavodoxin + 4 O2
-
 Bacillus subtilis 2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O overall reaction. Flavodoxins YkuN and YkuP support catalysis as kinetically competent redox partners. When an NADPH-utilizing bacterial flavodoxin reductase is added to reduce YkuP or YkuN, both support nitric oxide synthesis from either L-arginine or N-hydroxyarginine, with YkuN being more efficient ?

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.13.39 37
-
 assay at Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.13.39 7.6
-
 assay at Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.39 flavodoxin reduced YkuN and YkuP containing FMN, YkuN is more efficient in supporting bsNOS catalysis, Km for YkuN is 0.0016 mM, for YkuP 0.022 mM, overview Bacillus subtilis
1.14.13.39 heme
-
 Bacillus subtilis
1.14.13.39 NADPH
-
 Bacillus subtilis