Evidence for binding of NAD dimers to NAD-dependent dehydrogenases

Biochimica et Biophysica Acta (BBA) - Enzymology Pub Date : 1981-09-15 DOI:10.1016/0005-2744(81)90090-5

Alessandro Finazzi-Agrò , Luciana Avigliano , Vincenzo Carelli , Felice Liberatore , Antonio Casini

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引用次数: 11

Abstract

The binding of dimers of nicotinamide adenine dinucleotide, (NAD)₂, to lactate, malate and alcohol dehydrogenase has been studied by the fluorescence quenching technique. While the alcohol dehydrogenase shows a low binding ability, malate and lactate dehydrogenases have been found to bind (NAD)₂ in a specific way with high affinity. Malate dehydrogenase binds (NAD)₂ more than NADH. All three dehydrogenases are inhibited by (NAD)₂, which behaves as a competitive inhibitor with respect to both NAD⁺ and NADH. These results show that (NAD)₂ is bound to the nucleotide-specific binding site of the dehydrogenases. (NAD)₂ was found to stoichiometrically react with ferricyanide at variance with NADH. The specific interactions with the NAD-dependent dehydrogenases and the ability to enter in monoelectronic redox cycles suggest possible physiological roles for (NAD)₂.

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NAD二聚体与NAD依赖性脱氢酶结合的证据

采用荧光猝灭技术研究了烟酰胺腺嘌呤二核苷酸(NAD)2二聚体与乳酸、苹果酸和醇脱氢酶的结合。乙醇脱氢酶的结合能力较低，而苹果酸脱氢酶和乳酸脱氢酶则以高亲和力的特定方式结合NAD 2。苹果酸脱氢酶比NADH更能结合(NAD)2。这三种脱氢酶都被(NAD)2所抑制，而(NAD)2对于NAD+和NADH都是一种竞争性抑制剂。这些结果表明(NAD)2结合在脱氢酶的核苷酸特异性结合位点上。发现(NAD)2在不同的NADH下与铁氰化物发生化学计量反应。与NAD依赖性脱氢酶的特异性相互作用以及进入单电子氧化还原循环的能力表明(NAD)2可能具有生理作用。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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Biochimica et Biophysica Acta (BBA) - Enzymology

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