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Literature summary extracted from

  • Rusche, K.M.; Spiering, M.M.; Marletta, M.A.
    Reactions catalyzed by tetrahydrobiopterin-free nitric oxide synthase (1998), Biochemistry, 37, 15503-15512.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.39 expression in Escherichia coli, coexpression of calmodulin is necessary Mus musculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.13.39 CO
-
Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.39 0.036
-
Ngamma-hydroxy-L-arginine 25°C, with tetrahydrobiopterin Mus musculus
1.14.13.39 0.129
-
Ngamma-hydroxy-L-arginine 25°C, tetrahydrobiopterin-free Mus musculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.13.39 additional information 3 distinct isoforms: 1. a membrane-associated, constitutive enzyme from the vascular endothelium, 2. a soluble, constitutive enzyme from neuronal cells, 3. an endotoxin- and cytokine-inducible enzyme exemplified by that from murine macrophages Mus musculus
-
-
1.14.13.39 additional information activity of constitutive enzymes is regulated by binding of calmodulin and Ca2+, the inducible enzyme is regulated by binding of calmodulin, not by Ca2+ Mus musculus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.13.39 Iron protoporphyrin IX heme Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.39 Mus musculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.39 recombinant from Escherichia coli Mus musculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.13.39 macrophage RAW 264.7 cells Mus musculus
-
1.14.13.39 additional information 3 distinct isoforms: 1. a membrane-associated, constitutive enzyme from tha vascular endothelium, 2. a soluble, constitutive enzyme from neuronal cells, 3. an endotoxin- and cytokine-inducible enzyme exemplified by that from murine macrophages Mus musculus
-
1.14.13.39 additional information activity of constitutive enzymes is regulated by binding of calmodulin and Ca2+, the inducible enzyme is regulated by binding of calmodulin, not by Ca2+ Mus musculus
-

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 0.031
-
purified recombinant enzyme, NADPH/O2-supported reduction of Ngamma-hydroxy-L-arginine, tetrahydrobiopterin-free, 25°C Mus musculus
1.14.13.39 0.12
-
purified recombinant enzyme, H2O2-supported reduction of Ngamma-hydroxy-L-arginine, tetrahydrobiopterin-free, 25°C Mus musculus
1.14.13.39 0.17
-
purified recombinant enzyme, NADPH/O2-supported reduction of Ngamma-hydroxy-L-arginine, with tetrahydrobiopterin, 25°C Mus musculus
1.14.13.39 0.815
-
purified recombinant enzyme, H2O2-supported reduction of Ngamma-hydroxy-L-arginine, with tetrahydrobiopterin, 25°C Mus musculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.39 2 L-arginine + 3 NADPH + 4 O2 + 3 H+ tetrahydrobiopterin is absolutely required for partial reaction 1 Mus musculus 2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
?
1.14.13.39 Ngamma-hydroxy-L-arginine + H2O2 tetrahydrobiopterin-free Mus musculus citrulline + Ndelta-cyanoornithine + NO2- + NO3- NO2-/NO3- as aerobic decomposition products from NO- ?
1.14.13.39 Ngamma-hydroxy-L-arginine + NADPH + O2 substrate is intermediate between reaction 1 and 2 to form citrulline and NO from L-arginine Mus musculus citrulline + NADP+ + NO
-
?
1.14.13.39 Ngamma-hydroxy-L-arginine + NADPH + O2 reaction is possible without tetrahydrobiopterin, can also use H2O2 instead of NADPH and O2 Mus musculus citrulline + NADP+ + NO
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.13.39 25
-
assay at Mus musculus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.14.13.39 37
-
tetrahydrobiopterin-free enzyme is not stable, therefore reaction is performed at 25°C Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.39 5,6,7,8-tetrahydro-L-biopterin required Mus musculus
1.14.13.39 5,6,7,8-tetrahydro-L-biopterin required for the first partial reaction, formation of NG-hydroxy-L-arginine Mus musculus
1.14.13.39 FAD
-
Mus musculus
1.14.13.39 FMN
-
Mus musculus
1.14.13.39 NADPH
-
Mus musculus