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Membrane Binding and Substrate Access Merge in Cytochrome P450 7A1, a Key Enzyme in Degradation of Cholesterol
Journal of Biological Chemistry
To study membrane topology and mechanism for substrate specificity, we truncated residues 2-24 in microsomal cytochrome P450 7A1 (P450 7A1) and introduced conservative and nonconservative substitutions at positions 214 -227. Heterologous expression in Escherichia coli was followed by investigation of the subcellular distribution of the mutant P450s and determination of the kinetic and substrate binding parameters for cholesterol. The results indicate that a hydrophobic region, comprisingdoi:10.1074/jbc.m103943200 pmid:11423554 fatcat:upjkocyx4nhl5cl5sc4ndy3ko4