Cholesterol side-chain cleavage enzyme
mammalian protein found in Homo sapiens
Cholesterol side-chain cleavage enzyme is commonly referred to as P450scc, where "scc" is an abbreviation for side-chain cleavage, and more properly named CYP11A1. P450scc is a mitochondrial enzyme that catalyzes conversion of cholesterol to pregnenolone. This is the first reaction in the process of steroidogenesis in all mammalian tissues that specialize in the production of various steroid hormones.
P450scc is a member of the cytochrome P450 superfamily of enzymes (family 11, subfamily A, polypeptide 1) and is encoded by the CYP11A1 gene. The enzyme is sometimes referred to as cholesterol desmolase, due to the breaking of the carbon bonds (desmolysis).
Nomenclature
The systematic name of this enzyme class is cholesterol, reduced-adrenal-ferredoxin:oxygen oxidoreductase (side-chain-cleaving). Other names include:
Tissue and intracellular localization
The highest level of the cholesterol side-chain cleavage system is found in the adrenal cortex and the corpus luteum. The system is also expressed at high levels in steroidogenic theca cells in the ovary, and Leydig cells in the testis. During pregnancy, the placenta also expresses significant levels of this enzyme system. P450scc is also present at much lower levels in several other tissue types, including the brain.
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