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酿酒酵母钾激活醛脱氢酶的动力学及反应机制

Kinetics and reaction mechanism of potassium-activated aldehyde dehydrogenase from Saccharomyces cerevisiae.

作者信息

Bostian K A, Betts G F

出版信息

Biochem J. 1978 Sep 1;173(3):787-98. doi: 10.1042/bj1730787.

Abstract

Data from steady-state kinetic analysis of yeast K+-activated aldehyde dehydrogenase are consistent with a ternary complex mechanism. Evidence from alternative substrate analysis and product-inhibition studies supports an ordered sequence of substrate binding in which NAD+ is the leading substrate. A preincubation requirement for NAD+ for maximum activity is also consistent with the importance of a binary enzyme-NAD+ complex. Dissociation constant for enzyme-NAD+ complex determined kinetically is in reasonable agreement with that determined by direct binding. The order of substrate addition proposed here differs from that proposed for a yeast aldehyde dehydrogenase previously reported. Different methods of purification produced an enzyme that showed similar kinetic characteristics to those reported here.

摘要

酵母K⁺激活的醛脱氢酶稳态动力学分析的数据与三元复合物机制一致。来自替代底物分析和产物抑制研究的证据支持底物结合的有序序列,其中NAD⁺是主要底物。NAD⁺预孵育以达到最大活性的要求也与二元酶-NAD⁺复合物的重要性一致。通过动力学测定的酶-NAD⁺复合物的解离常数与通过直接结合测定的解离常数合理吻合。这里提出的底物添加顺序与先前报道的酵母醛脱氢酶的顺序不同。不同的纯化方法产生的一种酶,其动力学特征与这里报道的相似。

相似文献

8
Mitochondrial acetaldehyde dehydrogenase from Saccharomyces cerevisiae.来自酿酒酵母的线粒体乙醛脱氢酶。
Biochim Biophys Acta. 1974 Jun 18;350(2):277-91. doi: 10.1016/0005-2744(74)90502-6.

引用本文的文献

本文引用的文献

1
ON THE SITES OF ATTACHMENT AND REACTION OF ALDEHYDE DEHYDROGEN ASES.论醛脱氢酶的附着位点及反应
Proc Natl Acad Sci U S A. 1960 Feb;46(2):206-12. doi: 10.1073/pnas.46.2.206.
2
Yeast aldehyde dehydrogenase.酵母乙醛脱氢酶
Arch Biochem Biophys. 1951 Nov;34(1):86-97. doi: 10.1016/s0003-9861(51)80013-4.

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