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Information on EC 1.14.15.6 - cholesterol monooxygenase (side-chain-cleaving) and Organism(s) Mesocricetus auratus and UniProt Accession Q9EPT4

for references in articles please use BRENDA:EC1.14.15.6
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IUBMB Comments
A heme-thiolate protein (cytochrome P-450). The reaction proceeds in three stages, with two hydroxylations at C-22 and C-20 preceding scission of the side-chain between carbons 20 and 22. The initial source of the electrons is NADPH, which transfers the electrons to the adrenodoxin via EC 1.18.1.6, adrenodoxin-NADP+ reductase.
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This record set is specific for:
Mesocricetus auratus
UNIPROT: Q9EPT4
Word Map
The taxonomic range for the selected organisms is: Mesocricetus auratus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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+
6
reduced adrenodoxin
+
3
+
6
=
+
+
6
oxidized adrenodoxin
+
4
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C27-side chain cleavage enzyme
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cholesterol 20-22-desmolase
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cholesterol C20-22 desmolase
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cholesterol C20-C22 lyase
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cholesterol desmolase
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cholesterol side-chain cleavage enzyme
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cholesterol side-chain-cleaving enzyme
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CYPXIA1
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cytochrome P-450scc
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desmolase, steroid 20-22
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endoenzymes, cholesterol side-chain-cleaving
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enzymes, cholesterol side-chain-cleaving
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P450(scc)
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steroid 20-22 desmolase
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steroid 20-22-lyase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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SYSTEMATIC NAME
IUBMB Comments
cholesterol,reduced-adrenal-ferredoxin:oxygen oxidoreductase (side-chain-cleaving)
A heme-thiolate protein (cytochrome P-450). The reaction proceeds in three stages, with two hydroxylations at C-22 and C-20 preceding scission of the side-chain between carbons 20 and 22. The initial source of the electrons is NADPH, which transfers the electrons to the adrenodoxin via EC 1.18.1.6, adrenodoxin-NADP+ reductase.
CAS REGISTRY NUMBER
COMMENTARY hide
37292-81-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
25-hydroxycholesterol + reduced adrenodoxin + O2
pregnenolone + oxidized adrenodoxin + H2O
show the reaction diagram
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Swissprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
CP11A_MESAU
520
0
60271
Swiss-Prot
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vilchis, F.; Chavez, B.; Larrea, F.; Timossi, C.; Montiel, F.
The cDNA cloning and tissue expression of the cytochrome P450scc from Syrian hamster (Mesocricetus auratus)
Gen. Comp. Endocrinol.
126
279-286
2002
Mesocricetus auratus, Mesocricetus auratus (Q9EPT4)
Manually annotated by BRENDA team
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