钙离子、腺嘌呤核苷酸和pH对酿酒酵母和大鼠心脏线粒体NAD(+)-异柠檬酸脱氢酶及氧代戊二酸脱氢酶动力学特性影响的比较
Comparison of the effects of Ca2+, adenine nucleotides and pH on the kinetic properties of mitochondrial NAD(+)-isocitrate dehydrogenase and oxoglutarate dehydrogenase from the yeast Saccharomyces cerevisiae and rat heart.
作者信息
Nichols B J, Rigoulet M, Denton R M
机构信息
Department of Biochemistry, School of Medical Sciences, University of Bristol, UK.
出版信息
Biochem J. 1994 Oct 15;303 ( Pt 2)(Pt 2):461-5. doi: 10.1042/bj3030461.
Abstract
The regulatory properties of NAD(+)-isocitrate dehydrogenase and oxoglutarate dehydrogenase in extracts of yeast and rat heart mitochondria were studied under identical conditions. Yeast NAD(+)-isocitrate dehydrogenase exhibits a low K0.5 for isocitrate and is activated by AMP and ADP, but is insensitive to ATP and Ca2+. In contrast, the rat heart NAD(+)-isocitrate dehydrogenase was insensitive to AMP, but was activated by ADP and by Ca2+ in the presence of ADP or ATP. Both yeast and rat heart oxoglutarate dehydrogenase were stimulated by ADP, but only the heart enzyme was activated by Ca2+. All the enzymes studied were activated by decreases in pH, but to differing extents. The effects of Ca2+, adenine nucleotides and pH were through K0.5 for isocitrate or 2-oxoglutarate. These observations are discussed with reference to the deduced amino acid sequences of the constituent subunits of the enzymes, where they are available.
摘要
在相同条件下，研究了酵母和大鼠心脏线粒体提取物中NAD(+)-异柠檬酸脱氢酶和α-酮戊二酸脱氢酶的调节特性。酵母NAD(+)-异柠檬酸脱氢酶对异柠檬酸的K0.5较低，受AMP和ADP激活，但对ATP和Ca2+不敏感。相比之下，大鼠心脏NAD(+)-异柠檬酸脱氢酶对AMP不敏感，但在存在ADP或ATP的情况下受ADP和Ca2+激活。酵母和大鼠心脏的α-酮戊二酸脱氢酶均受ADP刺激，但只有心脏中的该酶受Ca2+激活。所研究的所有酶均受pH降低的激活，但程度不同。Ca2+、腺嘌呤核苷酸和pH的作用是通过对异柠檬酸或α-酮戊二酸的K0.5来实现的。文中参考了酶组成亚基的推导氨基酸序列（若有可用序列）对这些观察结果进行了讨论。
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