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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >On the reaction mechanism of L-lactate oxidase: Quantitative structure-activity analysis of the reaction with para-substituted-L-mandelates
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On the reaction mechanism of L-lactate oxidase: Quantitative structure-activity analysis of the reaction with para-substituted-L-mandelates

机译:关于L-乳酸氧化酶的反应机理:对-取代-L-扁桃酸酯反应的定量结构-活性分析

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摘要

The rate constants for reduction of the fla- voenzyme, L-lactate oxidase, and a mutant (in which alanine 95 is replaced by glycine), by a series of para-substituted mandelates, in both the 2-~1H- and 2-~2H- forms, have been measured by rapid reaction spectrophotometry. In all cases, significant isotope effects (~1H/~2H = 3-7) on the rate constants of flavin reduction were found, indicating that flavin reduc- tion is a direct measure of αC-H bond breakage. The rate constants show only a small influence of the electronic characteristics of the substituents, but show a good correla- tion when combined with some substituent volume parame- ters. A surprisingly good correlation is found with the molec- ular mass of the substrate.
机译:黄酮酶,L-乳酸氧化酶和突变体(其中丙氨酸95被甘氨酸替代),一系列的对位取代扁桃酸盐在2-〜1H-和2-H还原的速率常数已通过快速反应分光光度法测量了〜2H-形式。在所有情况下,均发现了对黄素还原速率常数的显着同位素影响(〜1H /〜2H = 3-7),这表明黄素还原是αC-H键断裂的直接量度。速率常数对取代基的电子特性影响很小,但与某些取代基体积参数结合时,则显示出良好的相关性。发现与底物的分子质量有着惊人的良好相关性。

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