Kinetic misinterpretation of a coupled enzyme reaction can lead to the assumption of an enzyme-enzyme interaction. The example of 3-phospho-D-glycerate kinase and glyceraldehyde-3-phosphate dehydrogenase couple.

Kinetic misinterpretation of a coupled enzyme reaction can lead to the assumption of an enzyme-enzyme interaction. The example of 3-phospho-D-glycerate kinase and glyceraldehyde-3-phosphate dehydrogenase couple.
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对偶联酶反应的动力学误解可能导致酶-酶相互作用的假设。

DOI:
10.1111/j.1432-1033.1990.tb19174.x
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发表时间:
1990
期刊:
European journal of biochemistry
影响因子:
--
通讯作者:
J. Batke
J. Batke
中科院分区:
--
文献类型:
--
作者:
M. Vas;J. Batke

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重新研究了3-磷酸- d -甘油激酶(GriP激酶)和甘油醛-3-磷酸脱氢酶(GraPDH)偶联催化3-磷酸-磷酸磷酸(GriP)转化为甘油醛-3-磷酸(GraP)的时间过程。稳态速率对脱氢酶浓度的依赖性与反应的连续性完全相容,因此不一定与两种酶的复合体形成有关。为了获得双酶复合物的Kd值,如Sukhodolets等人所做的[Sukhodolets, m.v., Muronetz, v.i. & Nagradova, n.k. (1987) Biochem]。Int. 15, 373-379],基本上是错误的。与以前的一些报道相反,GriP激酶的最大活性不受偶联分析系统中存在的辅助酶的影响。因此,GraPDH没有特殊的加速作用。与GriP激酶结合的1,3-双磷酸- d -甘油(GriP2)似乎不是GraPDH的底物,这为两种酶之间的GriP2通道提供了证据。
The time course of the conversion of 3-phospho-D-glycerate (GriP) to glyceraldehyde-3-phosphate (GraP) catalyzed by 3-phospho-D-glycerate kinase (GriP kinase) and glyceraldehyde-3-phosphate dehydrogenase (GraPDH) couple has been reinvestigated. The dependence of the steady-state rate on the dehydrogenase concentration is fully compatible with the consecutive nature of the reaction and therefore is not necessarily related to a complex formation of the two enzymes. To derive a Kd value of a bienzyme complex, as was done by Sukhodolets et al. [Sukhodolets, M. V., Muronetz, V. I. & Nagradova, N. K. (1987) Biochem. Int. 15, 373-379], is basically erroneous. In contrast with some previous reports, the maximal activity of GriP kinase is not influenced by the auxiliary enzyme present in the coupled assay system. Thus, no special accelerating effect can be attributed to GraPDH. 1,3-Bisphospho-D-glycerate (GriP2) bound to GriP kinase does not seem to be a substrate for GraPDH, providing evidence against channelling of GriP2 between the two enzymes.
酶-酶相互作用和代谢反应途径的调节。
DOI: 10.1016/b978-0-12-152828-7.50003-2
发表时间: 1986
期刊: Current topics in cellular regulation
影响因子: --
作者:
Srivastava,DK;Bernhard,SA
通讯作者: Bernhard,SA