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Literature summary extracted from

  • Klatt, P.; Heinzel, B.; John, M.; Kastner, M.; Böhme, E.; Mayer, B.
    Ca2+/calmodulin-dependent cytochrome c reductase activity of brain nitric oxide synthase (1992), J. Biol. Chem., 267, 11374-11378.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.13.39 nitroblue tetrazolium
-
 Sus scrofa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.39 0.008 0.0084 dichlorophenolindophenol
-
 Sus scrofa
1.14.13.39 0.016
-
 nitroblue tetrazolium
-
 Sus scrofa
1.14.13.39 0.0323 0.035 L-arginine cytochrome c reduction Sus scrofa

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.13.39 Ca2+ the enzyme bears Ca2+/calmodulin dependent cytochrome P-450 reductase activity which catalyzes cytochrome c reduction Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.39 additional information Sus scrofa NO represents the endogenous activator of soluble guanylyl cyclase ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.39 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.39
-
 Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.13.39 brain
-
 Sus scrofa
-
1.14.13.39 cerebellum
-
 Sus scrofa
-

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 0.01
-
 reductase activity Sus scrofa

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+
-
 Sus scrofa 2 L-citrulline + 2 NO + 3 NADP+ + 4 H2O the product is a guanylyl-cyclase-relaxing factor, that is identical with nitric oxide or a NO-releasing compound ?
1.14.13.39 2,6-dichlorophenolindophenol + NADPH + O2
-
 Sus scrofa ? + NO + NADP+
-
 ?
1.14.13.39 additional information the reductase domain has a broad substrate specificity, catalyzes a moderate Ca2+/calmodulin independent hydroxylation when the enzyme is reconstituted with purified P-450 Sus scrofa ?
-
 ?
1.14.13.39 additional information NO represents the endogenous activator of soluble guanylyl cyclase Sus scrofa ?
-
 ?
1.14.13.39 nitroblue tetrazolium + 2 NADPH
-
 Sus scrofa nitroblue tetrazolium formazan + 2 NADP+
-
 ?
1.14.13.39 oxidized cytochrome c + NADPH + O2 reaction is enhanced by addition of calmodulin at 0.0002 mM Sus scrofa reduced cytochrome c + NADP+ + H2O
-
 ?

Temperature Optimum [°C]

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.39 2,6-dichlorophenolindophenol activation Sus scrofa
1.14.13.39 5,6,7,8-tetrahydro-L-biopterin
-
 Sus scrofa
1.14.13.39 Calmodulin the enzyme bears a Ca2+/calmodulin dependent FAD and FMN containing reductase domain which transfers electrons from NADPH to a variety of acceptors Sus scrofa
1.14.13.39 cytochrome c activation Sus scrofa
1.14.13.39 FAD the enzyme bears Ca2+/calmodulin dependent FAD and FMN containing reductase domain which transfers electrons from NADPH to a variety of acceptors Sus scrofa
1.14.13.39 FMN the enzyme bears Ca2+/calmodulin dependent FAD and FMN containing reductase domain which transfers electrons from NADPH to a variety of acceptors Sus scrofa
1.14.13.39 NADPH
-
 Sus scrofa
1.14.13.39 nitroblue tetrazolium activation Sus scrofa