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Literature summary for 1.14.15.6 extracted from

  • Ahmed, S.
    The use of the novel substrate-heme complex approach in the derivation of a representation of the active site of the enzyme cholesterol side chain cleavage (2000), Biochem. Biophys. Res. Commun., 274, 821-824.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
additional information inhibitors bind to substrate-heme complex, longer chain compounds possess inhibitory activity, phenyl ethyl compounds not Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial inner membrane
-
Bos taurus 5743
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cholesterol + 6 reduced adrenodoxin + 3 O2 Bos taurus
-
pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O isocapraldehyde additional product ?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
adrenal cortex
-
Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cholesterol + 6 reduced adrenodoxin + 3 O2
-
Bos taurus pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin + 4 H2O isocapraldehyde additional product ?
cholesterol + reduced adrenodoxin + O2
-
Bos taurus pregnenolone + 4-methylpentanal + oxidized adrenodoxin + H2O
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Bos taurus

Cofactor

Cofactor Comment Organism Structure
adrenodoxin
-
Bos taurus
heme
-
Bos taurus
NADPH
-
Bos taurus