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Literature summary for 1.14.13.39 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
Search for more literature for 1.14.13.39

Cloned(Commentary)

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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

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

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 Drosophila melanogaster overall reaction, overview 2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
 ?
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

Organism UniProt Comment Textmining
Drosophila melanogaster
-
-
-

Purification (Commentary)

Purification (Comment) Organism
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)

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 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
-
 ?
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 overall reaction, overview Drosophila melanogaster 2 citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
-
 ?
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 ?
-
 ?
additional information a oxygenase domain of dNOS complex with ferrous heme-NO is relatively unreactive toward O2 Drosophila melanogaster ?
-
 ?
Nomega-hydroxy-L-arginine + NADPH + H+ + O2 second half reaction via intermediate Nomega-hydroxy-L-arginine Drosophila melanogaster citrulline + nitric oxide + NADP+ + H2O
-
 ?

Synonyms

Synonyms Comment Organism
DNOS
-
 Drosophila melanogaster
nitric oxide synthase
-
 Drosophila melanogaster

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

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