title: Cytochrome P450 side-chain cleavage: insights gained from homology modeling.
abstract: Cytochrome P450 side-chain cleavage (CYP11A1) catalyzes the conversion of cholesterol to pregnenolone, the first step in steroidogenesis. The absence of a solved crystal structure has complicated deductions pertaining to the structure/function relationships of this key enzyme. Although a number of techniques have been employed to identify domains and specific amino acid residues important for catalytic activity, these methods have been unsuccessful in predicting three-dimensional orientations in space and thus the mechanism by which they exert their kinetic effect. This review aims to demonstrate the significant contribution homology modelling, when employed as a tool in combination with other standard biochemical techniques, has made towards our understanding of CYP11A1.
authors.affiliation: Department of Biochemistry, University of Stellenbosch, Stellenbosch 7602, South Africa.
authors.forename: Karl-Heinz
authors.initials: KH
authors.lastname: Storbeck
authors.forename: Pieter
authors.initials: P
authors.lastname: Swart
authors.forename: Amanda C
authors.initials: AC
authors.lastname: Swart
mesh_terms: D000818:Animals; D002786:Cholesterol Side-Chain Cleavage Enzyme / Q000737:chemistry* / Q000378:metabolism*; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism; D006801:Humans; D051336:Mitochondrial Membranes / Q000201:enzymology / Q000378:metabolism; D008958:Models, Molecular; D011284:Pregnenolone / Q000378:metabolism; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D040681:Structural Homology, Protein
chemical_list: D011284:Pregnenolone; D003577:Cytochrome P-450 Enzyme System; D002786:Cholesterol Side-Chain Cleavage Enzyme