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Literature summary extracted from

  • Kuwada, M.; Ohsawa, Y.; Horie, S.
    Purification of NADPH-cytochrome c reductase from swine testis microsomes by chromatofocusing and characterization of the purified reductase (1985), Biochim. Biophys. Acta, 830, 45-51.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6.2.4 0.022
-
 NADPH
-
 Sus scrofa
1.6.2.4 0.057
-
 ferricytochrome c
-
 Sus scrofa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.6.2.4 microsome
-
 Sus scrofa
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.6.2.4 70000
-
 testis, gel filtration Sus scrofa

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.6.2.4
-
 Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.6.2.4 testis
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.6.2.4 26.1
-
-
 Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.2.4 2 ferricytochrome c + NADPH
-
 Sus scrofa 2 ferrocytochrome c + NADP+ + H+
-
 ?
1.6.2.4 ferricytochrome c + NADPH + H+
-
 Sus scrofa ferrocytochrome c + NADP+
-
 r

Subunits

EC Number Subunits Comment Organism
1.6.2.4 ? x * 72000-87000, SDS-PAGE Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.2.4 FAD ratio FAD : FMN 1 : 1 Sus scrofa
1.6.2.4 FMN ratio FAD : FMN 1 : 1 Sus scrofa
1.6.2.4 NADPH
-
 Sus scrofa