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结构和光谱研究揭示了草酸氧化酶的作用机制。

Structural and spectroscopic studies shed light on the mechanism of oxalate oxidase.

作者信息

Opaleye Olaniyi, Rose Ruth-Sarah, Whittaker Mei M, Woo Eui-Jeon, Whittaker James W, Pickersgill Richard W

机构信息

School of Biological and Chemical Sciences, Queen Mary, University of London, Mile End Road, London E1 4NS, United Kingdom.

出版信息

J Biol Chem. 2006 Mar 10;281(10):6428-33. doi: 10.1074/jbc.M510256200. Epub 2005 Nov 15.

Abstract

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

摘要

草酸氧化酶(EC 1.2.3.4)催化草酸和双氧生成过氧化氢和二氧化碳的反应。在本研究中,乙醇酸被用作草酸的结构类似物,以研究结晶酶中的底物结合情况。观察到的乙醇酸与草酸氧化酶活性位点锰离子的单齿结合,与一种涉及超氧阴离子攻击单齿配位底物驱动C-C键断裂的机制相一致。在该机制中,金属发挥两种功能:组织底物(草酸和双氧)以及短暂还原双氧。观察到的结构进一步表明,特定活性位点残基(两个天冬酰胺和一个谷氨酰胺)在正确定向底物和反应中间体以进行催化方面发挥着重要作用。对突变体进行的光谱、生化和结构联合分析证实了天冬酰胺残基在构建功能性活性位点复合物中的重要性。

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