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。
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