作者: Alice Vrielink , Sandro Ghisla
DOI: 10.1111/J.1742-4658.2009.07377.X
关键词: Biochemistry 、 Substrate (chemistry) 、 Chemistry 、 Active site 、 Protein structure 、 Flavin group 、 Cholesterol oxidase 、 Enzyme kinetics 、 Cofactor 、 Enzyme
摘要: Cholesterol oxidases are bifunctional flavoenzymes that catalyze the oxidation of steroid substrates which have a hydroxyl group at 3β position ring system. The enzyme is found, in wide range bacterial species, two forms: one with FAD cofactor bound noncovalently to enzyme; and linked covalently protein. Here we discuss, compare contrast salient biochemical properties forms enzyme. Specifically, structural features discussed affect redox potentials flavin cofactor, chemical mechanism substrate dehydrogenation by active-center amino acid residues, kinetic parameters both types enzymes reactivity reduced molecular dioxygen. presence tunnel proposed serve access dioxygen active site mechanisms its control ‘gate’ formed residues highlighted.