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Literature summary for 1.6.2.4 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
Search for more literature for 1.6.2.4

KM Value [mM]

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

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
 Sus scrofa
-
-

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
testis
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

Cofactor

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