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Literature summary for 1.14.13.39 extracted from

  • Ghosh, D.K.; Holliday, M.A.; Thomas, C.; Weinberg, J.B.; Smith, S.M.; Salerno, J.C.
    Nitric-oxide synthase output state. Design and properties of nitric-oxide synthase oxygenase/FMN domain constructs (2006), J. Biol. Chem., 281, 14173-14183.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Ca2+/calmodulin calmodulin activates electron transfer from NADPH through three reductase domains to the oxygenase domain, controls constitutive isoforms through regulation of electron transfer between NADPH and heme Rattus norvegicus
Ca2+/calmodulin calmodulin activates electron transfer from NADPH through three reductase domains to the oxygenase domain, controls constitutive isoforms through regulation of electrontransfer between NADPH and heme Mus musculus
Ca2+/calmodulin calmodulin activates electron transfer from NADPH through three reductase domains to the oxygenase domain, controls constitutive isoforms through regulation of electrontransfer between NADPH and heme Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+/calmodulin calmodulin activates electron transfer from NADPH through three reductase domains to the oxygenase domain, controls constitutive isoforms through regulation of electron transfer between NADPH and heme Rattus norvegicus
Ca2+/calmodulin calmodulin activates electron transfer from NADPH through three reductase domains to the oxygenase domain, controls constitutive isoforms through regulation of electrontransfer between NADPH and heme Mus musculus
Ca2+/calmodulin calmodulin activates electron transfer from NADPH through three reductase domains to the oxygenase domain, controls constitutive isoforms through regulation of electrontransfer between NADPH and heme Homo sapiens
Iron heme iron, FMN/heme electron transfer Mus musculus
Iron heme iron, FMN/heme electron transfer Rattus norvegicus
Iron heme iron, FMN/heme electron transfer Homo sapiens
Zn2+ bound by Cys104, Cys109, and Cys194 of isozyme iNOS oxygenase domain Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
69000
-
2 * 69000, iNOS, SDS-PAGE Mus musculus
75000
-
2 * 75000, nNOS, SDS-PAGE Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 L-arginine + 3 NADPH + 4 O2 + 3 H+ Mus musculus
-
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+ Rattus norvegicus
-
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+ Homo sapiens
-
2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
?
additional information Mus musculus calmodulin-controlled isoforms are signal generators, overview ?
-
?
additional information Rattus norvegicus calmodulin-controlled isoforms are signal generators, overview ?
-
?
additional information Homo sapiens calmodulin-controlled isoforms are signal generators, overview ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P29474 isozyme eNOS
-
Mus musculus
-
isozyme iNOS
-
Rattus norvegicus P29476 isozyme nNOS
-

Reaction

Reaction Comment Organism Reaction ID
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O interaction and electrontransfer between enzyme domains and bound cofactors calmodulin, FMN, FAD, tetrahydrobiopterin, heme, and NADPH, overview Mus musculus
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O interaction and electrontransfer between enzyme domains and bound cofactors calmodulin, FMN, FAD, tetrahydrobiopterin, heme, and NADPH, overview Rattus norvegicus
2 L-arginine + 3 NADPH + 3 H+ + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O interaction and electrontransfer between enzyme domains and bound cofactors calmodulin, FMN, FAD, tetrahydrobiopterin, heme, and NADPH, overview Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Rattus norvegicus
-
endothelium
-
Homo sapiens
-
macrophage
-
Mus musculus
-
neuron
-
Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
-
Mus musculus 2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
-
Rattus norvegicus 2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
?
2 L-arginine + 3 NADPH + 4 O2 + 3 H+
-
Homo sapiens 2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O
-
?
additional information calmodulin-controlled isoforms are signal generators, overview Mus musculus ?
-
?
additional information calmodulin-controlled isoforms are signal generators, overview Rattus norvegicus ?
-
?
additional information calmodulin-controlled isoforms are signal generators, overview Homo sapiens ?
-
?
additional information both oxyFMN and oxygenase domain activity are measured by following H2O2-supported oxidation of Nomega-hydroxy-L-Arg, L-NOHA, overview Mus musculus ?
-
?
additional information both oxyFMN and oxygenase domain activity are measured by following H2O2-supported oxidation of Nomega-hydroxy-L-Arg, L-NOHA, overview Rattus norvegicus ?
-
?
additional information both oxyFMN and oxygenase domain activity are measured by following H2O2-supported oxidation of Nomega-hydroxy-L-Arg, L-NOHA, overview Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
dimer
-
Homo sapiens
dimer 2 * 69000, iNOS, SDS-PAGE Mus musculus
dimer 2 * 75000, nNOS, SDS-PAGE Rattus norvegicus

Synonyms

Synonyms Comment Organism
endothelial nitric oxide synthase
-
Homo sapiens
eNOS
-
Homo sapiens
inducible nitric oxide synthase
-
Mus musculus
iNOS
-
Mus musculus
neuronal nitric oxide synthase
-
Rattus norvegicus
nNOS
-
Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Mus musculus
37
-
assay at Rattus norvegicus
37
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
assay at Mus musculus
7.6
-
assay at Rattus norvegicus
7.6
-
assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD
-
Mus musculus
FAD
-
Rattus norvegicus
FAD
-
Homo sapiens
FMN FMN/heme electron transfer, FMN is capable of serving as a one electron heme reductant Mus musculus
FMN FMN/heme electron transfer, FMN is capable of serving as a one electron heme reductant Rattus norvegicus
FMN FMN/heme electron transfer, FMN is capable of serving as a one electron heme reductant Homo sapiens
NADPH
-
Mus musculus
NADPH
-
Rattus norvegicus
NADPH
-
Homo sapiens