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Literature summary extracted from

  • Ray, S.S.; Tejero, J.; Wang, Z.Q.; Dutta, T.; Bhattacharjee, A.; Regulski, M.; Tully, T.; Ghosh, S.; Stuehr, D.J.
    Oxygenase domain of Drosophila melanogaster nitric oxide synthase: unique kinetic parameters enable a more efficient NO release (2007), Biochemistry, 46, 11857-11864.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.39 expression of His-tagged dNOS in Escherichia coli Drosophila melanogaster

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 modeling and single-turnover reactions, kinetics of heme transitions during Arg oxidation, product stoichiometry analysis, detailed overview Drosophila melanogaster

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.13.39 Ca2+ dependent on Drosophila melanogaster
1.14.13.39 Fe2+ a heme enzyme Drosophila melanogaster

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 Drosophila melanogaster overall reaction, overview 2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
 ?
1.14.13.39 additional information Drosophila melanogaster Drosophila dNOS is a more efficient and active NO synthase than the mammalian NOS enzymes, which may allow it to function more broadly in cell signaling and immune functions in the fruit fly ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.39 Drosophila melanogaster
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.39 recombinant His-tagged dNOS from Escherichia coli by nickel affinity and anion exchange chromatography in the presence of L-Arg and H4B Drosophila melanogaster

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 with consecutive appearance of heme-dioxy, ferric heme-NO, and ferric heme species, overview Drosophila melanogaster 2 Nomega-hydroxy-L-arginine + 2 NADP+ + 2 H2O
-
 ?
1.14.13.39 2 L-arginine + 3 NADPH + 3 H+ + 4 O2 overall reaction, overview Drosophila melanogaster 2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
 ?
1.14.13.39 additional information Drosophila dNOS is a more efficient and active NO synthase than the mammalian NOS enzymes, which may allow it to function more broadly in cell signaling and immune functions in the fruit fly Drosophila melanogaster ?
-
 ?
1.14.13.39 additional information a oxygenase domain of dNOS complex with ferrous heme-NO is relatively unreactive toward O2 Drosophila melanogaster ?
-
 ?
1.14.13.39 Nomega-hydroxy-L-arginine + NADPH + H+ + O2 second half reaction via intermediate Nomega-hydroxy-L-arginine Drosophila melanogaster citrulline + nitric oxide + NADP+ + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.13.39 DNOS
-
 Drosophila melanogaster
1.14.13.39 nitric oxide synthase
-
 Drosophila melanogaster

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.13.39 10
-
 assay at Drosophila melanogaster

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.13.39 7.5 7.6 assay at Drosophila melanogaster

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.39 (6R)-tetrahydrobiopterin required Drosophila melanogaster
1.14.13.39 Calmodulin dependent on Drosophila melanogaster
1.14.13.39 heme
-
 Drosophila melanogaster
1.14.13.39 NADPH
-
 Drosophila melanogaster