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如何确定相互作用的酶系统中中间传递的效率?

How to determine the efficiency of intermediate transfer in an interacting enzyme system?

作者信息

Tompa P, Batke J, Ovádi J

出版信息

FEBS Lett. 1987 Apr 20;214(2):244-8. doi: 10.1016/0014-5793(87)80063-7.

DOI:10.1016/0014-5793(87)80063-7
PMID:3569522
Abstract

A kinetic method, based upon measuring the transient time of coupled reactions, is proposed for the determination of the intermediate channel efficiency in a system of functionally interacting enzymes. The procedure rests upon a novel description in which the transient time is expressed as a function of channel efficiency and lifetime of the intermediate molecules. By this approach the reduction of transient time can be explained even if no changes in the kinetic parameters of the individual reactions occur. For determining channel efficiency, a linearized form has been evaluated and applied to the analysis of the kinetics of the aspartate aminotransferase-glutamate dehydrogenase coupled reaction, for which the data were taken from the literature [(1982) Eur. J. Biochem. 121, 511-517].

摘要

提出了一种基于测量偶联反应瞬态时间的动力学方法,用于测定功能相互作用酶系统中的中间通道效率。该方法基于一种新颖的描述,其中瞬态时间表示为通道效率和中间分子寿命的函数。通过这种方法,即使各个反应的动力学参数没有变化,也可以解释瞬态时间的减少。为了确定通道效率,已经评估了一种线性化形式,并将其应用于天冬氨酸转氨酶-谷氨酸脱氢酶偶联反应的动力学分析,其数据取自文献[(1982) Eur. J. Biochem. 121, 511-517]。

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1
How to determine the efficiency of intermediate transfer in an interacting enzyme system?如何确定相互作用的酶系统中中间传递的效率?
FEBS Lett. 1987 Apr 20;214(2):244-8. doi: 10.1016/0014-5793(87)80063-7.
2
Kinetics of coupled reactions catalyzed by aspartate aminotransferase and glutamate dehydrogenase.
Eur J Biochem. 1982 Jan;121(3):511-7. doi: 10.1111/j.1432-1033.1982.tb05816.x.
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Coupled reaction of immobilized aspartate aminotransferase and malate dehydrogenase. A plausible model for the cellular behaviour of these enzymes.固定化天冬氨酸转氨酶与苹果酸脱氢酶的偶联反应。这些酶细胞行为的一种合理模型。
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Aminotransferase-glutamate dehydrogenase-carbamyl phosphate synthase-I interactions.
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Nanosecond emission anisotropy of interacting enzymes aspartate aminotransferase glutamate dehydrogenase.
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The anomalous kinetics of coupled aspartate aminotransferase and malate dehydrogenase. Evidence for compartmentation of oxaloacetate.天冬氨酸转氨酶与苹果酸脱氢酶偶联反应的异常动力学。草酰乙酸区室化的证据。
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Analysis of progress curves for enzyme-catalyzed reactions: application to unstable enzymes, coupled reactions and transient-state kinetics.酶催化反应进程曲线分析:在不稳定酶、偶联反应及瞬态动力学中的应用
Biochim Biophys Acta. 1994 Apr 13;1205(2):268-74. doi: 10.1016/0167-4838(94)90244-5.

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Int J Mol Sci. 2012;13(2):1858-1885. doi: 10.3390/ijms13021858. Epub 2012 Feb 10.
2
Transient-time analysis of substrate-channelling in interacting enzyme systems.相互作用酶系统中底物通道化的瞬态时间分析。
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