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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)

Subunits

Subunits on EC 1.14.15.6 - cholesterol monooxygenase (side-chain-cleaving)

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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexadecamer
-
16 * 53000, sedimentation equilibrium performed in 6 M guanidine after heating, 16 * 52000, SDS-PAGE. Can also exist in forms of 4 and 8 subunits after treatment with 100 mM potassium phosphate buffer, 7.6, with molecular weights of 200000 and 470000, respectively
tetramer
-
4 * 46000, sedimentation equilibrium analysis after guanidine treatment and SDS-PAGE
additional information
-
the enzyme structure possesses a substrate access channel, the F-G loop is a membrane-interacting area