作者: Olaniyi Opaleye , Ruth-Sarah Rose , Mei M. Whittaker , Eui-Jeon Woo , James W. Whittaker
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摘要: Oxalate oxidase (EC 1.2.3.4) catalyzes the conversion of oxalate and dioxygen to hydrogen peroxide carbon dioxide. In this study, glycolate was used as a structural analogue investigate substrate binding in crystalline enzyme. The observed monodentate active site manganese ion is consistent with mechanism involving C-C bond cleavage driven by superoxide anion attack on coordinated substrate. mechanism, metal serves two functions: organize substrates (oxalate dioxygen) transiently reduce dioxygen. structure further implies important roles for specific residues (two asparagines one glutamine) correctly orientating reaction intermediates catalysis. Combined spectroscopic, biochemical, analyses mutants confirms importance asparagine organizing functional complex.