Cholesterol side-chain cleavage enzyme

Cholesterol side-chain cleavage enzyme is commonly referred to as P450scc, where "scc" is an acronym for side-chain cleavage. 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). The gene name is CYP11A1.

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. In the adrenal cortex, the concentration of adrenodoxin is similar to that of P450scc, but adrenodoxin reductase is expressed at lower levels.