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1.14.15.6: cholesterol monooxygenase (side-chain-cleaving)

This is an abbreviated version!
For detailed information about cholesterol monooxygenase (side-chain-cleaving), go to the full flat file.

Word Map on EC 1.14.15.6

Reaction

(20R,22R)-20,22-dihydroxy-cholesterol
+ 2 reduced adrenodoxin +
O2
+ 2 H+ =
pregnenolone
+
4-Methylpentanal
+ 2 oxidized adrenodoxin + 2 H2O

Synonyms

C27-side chain cleavage enzyme, cholesterol 20-22-desmolase, cholesterol C20-22 desmolase, cholesterol C20-C22 lyase, cholesterol desmolase, cholesterol hydroxylase, cholesterol side chain cleavage cytochrome P450, cholesterol side chain cleavage enzyme, cholesterol side-chain cleavage cytochrome P450, cholesterol side-chain cleavage cytochrome P450 enzyme, cholesterol side-chain cleavage enzyme, cholesterol side-chain-cleaving enzyme, cholesterol side-cleaving enzyme, CYP 11A1, Cyp11a, CYP11A1, CYPXIA1, cytochrome P-450scc, cytochrome P450 11A1, cytochrome P450 cholesterol side chain cleavage, cytochrome P450 cholesterol side-chain cleavage, cytochrome P450 side chain cleavage enzyme, cytochrome P450-mediated cholesterol side-chain cleavage enzyme, cytochrome P450-mediated side-chain cleavage enzyme, cytochrome P450scc, desmolase, steroid 20-22, endoenzymes, cholesterol side-chain-cleaving, enzymes, cholesterol side-chain-cleaving, P450 11A1, P450 cholesterol side chain cleaving enzyme, P450 cholesterol side-chain cleavage enzyme, P450(scc), P450scc, steroid 20-22 desmolase, steroid 20-22-lyase

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.15.6 cholesterol monooxygenase (side-chain-cleaving)

General Information

General Information on EC 1.14.15.6 - cholesterol monooxygenase (side-chain-cleaving)

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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
additional information
the active site cavity in CYP11A1 represents a long curved tube that extends from the protein surface to the heme group, the site of catalysis. Shuttling of the sterol intermediates between the active site entrance and the heme group during the three-step reaction. Structural basis of the strict substrate specificity and high catalytic efficiency of the enzyme, overview