A-B脱氢酶系统中缺乏直接辅酶转移。
Absence of direct coenzyme transfer in an A-B dehydrogenase system.
作者信息
Ehrlich R S
机构信息
Department of Chemistry and Biochemistry, University of Delaware, Newark 19716.
出版信息
Biochem J. 1987 Nov 15;248(1):269-71. doi: 10.1042/bj2480269.
Abstract
Direct transfer of NADPH between two NADP-dependent dehydrogenases, isocitrate dehydrogenase and glutamate dehydrogenase, has been investigated. These enzymes have opposite stereospecificity for hydrogen transfer to the coenzyme. In contrast with the general direct-transfer mechanism postulated for NAD-dependent dehydrogenases [Srivastava & Bernhard (1986) Science 234, 1081-1086], no evidence for direct transfer in either direction was found for these NADP-dependent dehydrogenases.
摘要
已经对烟酰胺腺嘌呤二核苷酸磷酸（NADPH）在两种依赖于NADP的脱氢酶（异柠檬酸脱氢酶和谷氨酸脱氢酶）之间的直接转移进行了研究。这些酶在将氢转移到辅酶时具有相反的立体特异性。与为依赖于NAD的脱氢酶所假定的一般直接转移机制[斯里瓦斯塔瓦和伯恩哈德（1986年）《科学》234, 1081 - 1086]相反，对于这些依赖于NADP的脱氢酶，未发现任何一个方向上直接转移的证据。
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