KEGG   ENZYME: 1.14.15.6Help
Entry
EC 1.14.15.6                Enzyme                                 

Name cholesterol monooxygenase (side-chain-cleaving);
cholesterol desmolase;
cytochrome P-450scc;
desmolase, steroid 20-22;
C27-side chain cleavage enzyme;
cholesterol 20-22-desmolase;
cholesterol C20-22 desmolase;
cholesterol side-chain cleavage enzyme;
cholesterol side-chain-cleaving enzyme;
enzymes, cholesterol side-chain-cleaving;
steroid 20-22 desmolase;
steroid 20-22-lyase
Class Oxidoreductases;
Acting on paired donors, with O2 as oxidant and incorporation or
reduction of oxygen. The oxygen incorporated need not be derived
from O2;
With reduced iron-sulfur protein as one donor, and incorporation of
one atom of oxygen into the other donor
BRITE hierarchy
Sysname cholesterol,reduced-adrenal-ferredoxin:oxygen oxidoreductase
(side-chain-cleaving)
Reaction(IUBMB) cholesterol + reduced adrenal ferredoxin + O2 = pregnenolone +
4-methylpentanal + oxidized adrenal ferredoxin + H2O [RN:R02724]
Reaction(KEGG) R02724;
(other) R01454 R02723 R03933 R04676 R04854 R04855
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Substrate cholesterol [CPD:C00187];
reduced adrenal ferredoxin [CPD:C00662];
O2 [CPD:C00007]
Product pregnenolone [CPD:C01953];
4-methylpentanal [CPD:C02373];
oxidized adrenal ferredoxin [CPD:C00667];
H2O [CPD:C00001]
Cofactor Heme [CPD:C00032]
Comment A heme-thiolate protein. The reaction proceeds in three stages, with
hydroxylation at C-20 and C-22 preceding scission of the side-chain
at C-20.
Pathway PATH: ec00140  Steroid hormone biosynthesis
PATH: ec01100  Metabolic pathways
Orthology KO: K00498  cytochrome P450, family 11, subfamily A (cholesterol
            monooxygenase (side-chain-cleaving))
Genes HSA: 1583(CYP11A1)
PTR: 748998
MCC: 708065
MMU: 13070(Cyp11a1)
RNO: 29680(Cyp11a1)
CFA: 478365
BTA: 338048(CYP11A1)
SSC: 403329(CYP11A1)
ECB: 100034229(P450SCC)
MDO: 100029519
GGA: 414838(CYP11A1)
TGU: 100151695(CYP11A1)
DRE: 563363 80374(cyp11a1)
Taxonomy
Reference
  Authors
  Title

  Journal
1  [PMID:6766943]
Hanukoglu I, Jefcoate CR.
Mitochondrial cytochrome P-450sec. Mechanism of electron transport
by adrenodoxin.
J. Biol. Chem. 255 (1980) 3057-61.
Reference
  Authors
  Title

  Journal
  Organism
2  [PMID:7217084]
Hanukoglu I, Spitsberg V, Bumpus JA, Dus KM, Jefcoate CR.
Adrenal mitochondrial cytochrome P-450scc. Cholesterol and
adrenodoxin interactions at equilibrium and during turnover.
J. Biol. Chem. 256 (1981) 4321-8.
Bos taurus [GN:bta]
Other DBs ExplorEnz - The Enzyme Database: 1.14.15.6
IUBMB Enzyme Nomenclature: 1.14.15.6
ExPASy - ENZYME nomenclature database: 1.14.15.6
BRENDA, the Enzyme Database: 1.14.15.6
CAS: 37292-81-2 440354-98-3

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