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Literature summary for 1.6.2.4 extracted from

  • Ichihara, K.; Kusunose, E.; Kusunose, M.
    Some properties of NADPH-cytochrome c reductase reconstitutively active in fatty-acid omega-hydroxylation (1973), Eur. J. Biochem., 38, 463-472.
    View publication on PubMed

Localization

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
liver microsomes, gel filtration Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
chromatography in DEAE-cellulose, DEAE-Sephadex A-50 and hydroxylapatite Sus scrofa

Renatured (Commentary)

Renatured (Comment) Organism
reconstitution of laurate omega-hydroxylation activity Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.5
-
preparative polyacrylamide disc gel electrophoresis Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricytochrome c + NADPH additional electron acceptor: neotetrazolium chloride Sus scrofa 2 ferrocytochrome c + NADP+ + H+
-
?
2 ferricytochrome c + NADPH additional electron acceptor: cytochrome P450 Sus scrofa 2 ferrocytochrome c + NADP+ + H+
-
?
additional information omega-hydroxylation of fatty acids together with cytochrome P450 Sus scrofa ?
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
stable in a frozen state at least for one month Sus scrofa

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Sus scrofa