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哺乳动物D-2-羟基酸脱氢酶。抑制剂的作用及反应顺序。

Mammalian D-2-hydroxy acid dehydrogenase. Effect of inhibitors and reaction sequence.

作者信息

Cammack R

出版信息

Biochem J. 1970 Jul;118(3):405-8. doi: 10.1042/bj1180405.

DOI:10.1042/bj1180405
PMID:5528639
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1179206/
Abstract
  1. The reaction of d-2-hydroxy acid dehydrogenase with d-lactate and 2,6-dichlorophenol-indophenol (DCIP) at pH8.6 yields reciprocal plots of 1/rate versus 1/[d-lactate], at different DCIP concentrations, which appear to be parallel. However, at pH7.55, or in the presence of the competitive inhibitor oxalate at pH8.6, the plots are convergent. This is inconsistent with the mechanism previously proposed for this enzyme. 2. The pattern of inhibition by the product, pyruvate, is consistent with either an Ordered mechanism or an Iso Theorell-Chance mechanism. 3. The observation that the enzyme forms a complex with d-lactate favours the Ordered reaction. In this, first d-lactate and then DCIP bind to the enzyme to form a ternary complex, from which pyruvate and reduced DCIP dissociate in that order.
摘要
  1. 在pH8.6条件下,d - 2 - 羟基酸脱氢酶与d - 乳酸和2,6 - 二氯酚靛酚(DCIP)反应,在不同DCIP浓度下,得到1/速率对1/[d - 乳酸]的倒数图,这些图似乎是平行的。然而,在pH7.55时,或在pH8.6条件下存在竞争性抑制剂草酸盐时,这些图是收敛的。这与先前提出的该酶作用机制不一致。2. 产物丙酮酸的抑制模式与有序机制或Iso Theorell - Chance机制一致。3. 酶与d - 乳酸形成复合物这一观察结果支持有序反应。在此反应中,首先d - 乳酸然后DCIP与酶结合形成三元复合物,丙酮酸和还原型DCIP按此顺序从中解离。

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引用本文的文献

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From Glucose to Lactate and Transiting Intermediates Through Mitochondria, Bypassing Pyruvate Kinase: Considerations for Cells Exhibiting Dimeric PKM2 or Otherwise Inhibited Kinase Activity.从葡萄糖到乳酸以及通过线粒体的过渡中间体,绕过丙酮酸激酶:对表现出二聚体PKM2或其他激酶活性受抑制的细胞的考量
Front Physiol. 2020 Dec 1;11:543564. doi: 10.3389/fphys.2020.543564. eCollection 2020.

本文引用的文献

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The kinetics of enzyme-catalyzed reactions with two or more substrates or products. II. Inhibition: nomenclature and theory.具有两种或更多种底物或产物的酶催化反应动力学。II. 抑制作用:命名法与理论
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The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations.具有两种或更多种底物或产物的酶催化反应动力学。I. 命名法和速率方程。
Biochim Biophys Acta. 1963 Jan 8;67:104-37. doi: 10.1016/0006-3002(63)91800-6.
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Studies on the mechanism of enzyme-catalyzed oxidation-reduction reactions. VI. Kinetic studies with yeast L-lactate dehydrogenase.酶催化氧化还原反应机制的研究。VI. 酵母L-乳酸脱氢酶的动力学研究。
Biochemistry. 1963 Mar-Apr;2:209-16. doi: 10.1021/bi00902a001.
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Effects of inhibitors on mitochondrial D-alpha-hydroxy acid dehydrogenase.抑制剂对线粒体D-α-羟酸脱氢酶的影响。
Biochem J. 1962 Jan;82(1):36-42. doi: 10.1042/bj0820036.
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The oxidation of D-alpha-hydroxy acids in animal tissues.动物组织中D-α-羟基酸的氧化作用。
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Preparation and properties of highly purified diaphorase.高纯度黄递酶的制备及性质
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Studies on succinate dehydrogenase. IV. Kinetics of the overall reaction catalysed by preparations of the purified enzyme.
Biochim Biophys Acta. 1969 Apr 22;178(2):213-24. doi: 10.1016/0005-2744(69)90391-x.
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