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[动物源α-酮戊二酸脱氢酶复合体活性的调节(综述)]

[Regulation of the activity of the oxoglutarate dehydrogenase complex of animal origin (review)].

作者信息

Strumilo S A

出版信息

Vopr Med Khim. 1988 Mar-Apr;34(2):2-7.

PMID:3041670
Abstract

Recent data on regulation of the multi-enzyme oxoglutarate dehydrogenase complex from pigeon breast muscle, porcine heart, bovine adrenal glands and kidney are reviewed. The most characteristic property of the complex consists in activation of the trigger oxoglutarate dehydrogenase component by and ATP. Action of these agents is more pronounced at low concentrations of 2-oxoglutarate and is directed towards alteration of the substrate half-saturation value SO.5. The adrenal oxoglutarate dehydrogenase complex exhibits positive cooperativity of allosteric ADP-binding sites which improved its sensitivity to variations in the effector concentration. The oxoglutarate dehydrogenase complex appears to be not only an important functional component but also is a regulatory unit of the Krebs cycle.

摘要

本文综述了近期关于鸽胸肌、猪心、牛肾上腺和肾脏中多酶α-酮戊二酸脱氢酶复合体调控的研究数据。该复合体最显著的特性是ATP对触发酶α-酮戊二酸脱氢酶组分的激活作用。这些物质在低浓度α-酮戊二酸时作用更为明显,其作用方向是改变底物半饱和值SO.5。肾上腺α-酮戊二酸脱氢酶复合体表现出变构ADP结合位点的正协同性,这提高了其对效应物浓度变化的敏感性。α-酮戊二酸脱氢酶复合体似乎不仅是一个重要的功能组分,也是三羧酸循环的一个调节单元。

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