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Literature summary for 1.14.14.23 extracted from

  • Miki, N.; Miura, R.; Miyake, Y.
    Purification and characterization of cholesterol 7alpha-hydroxylase cytochrome P-450 of untreated rabbit liver microsomes (1987), J. Biochem., 101, 1087-1094.
    View publication on PubMed
Search for more literature for 1.14.14.23

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
 Oryctolagus cuniculus
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 MW of cytochrome P-450: 48000, SDS-PAGE Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
 enzyme complex reconstituted from cytochrome b5
-
Oryctolagus cuniculus
-
 enzyme complex reconstituted from cytochrome P-450, NADPH-cytochrome P-450 reductase
-

Purification (Commentary)

Purification (Comment) Organism
purification of cytochrome P-450 Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cholesterol + [reduced NADPH-hemoprotein reductase] + O2
-
 Oryctolagus cuniculus 7alpha-hydroxycholesterol + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?
additional information specificity of reconstituted enzyme system Oryctolagus cuniculus ?
-
 ?

Cofactor

Cofactor Comment Organism Structure
cytochrome b5 essential component of the cholesterol 7alpha-hydroxylase system Oryctolagus cuniculus
NADPH
-
 Oryctolagus cuniculus