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NAD+及其结构成分的自旋标记衍生物的合成及其与乳酸脱氢酶的结合。

The synthesis of spin-label derivatives of NAD+ and its structural components and their binding to lactate dehydrogenase.

作者信息

Wenzel H R, Pfleiderer G, Trommer W E, Paschenda K, Redhardt A

出版信息

Biochim Biophys Acta. 1976 Dec 8;452(2):292-301. doi: 10.1016/0005-2744(76)90179-0.

DOI:10.1016/0005-2744(76)90179-0
PMID:188462
Abstract

Spin-labelled derivatives of NAD+ and its structural components (i.e. adenosine, adenine, AMP, ADP and ADPR) have been synthesized. Their binding to pig heart lactate dehydrogenase (L-lactate:NAD+ oxidoreductase, EC 1.1.1.27) has been studied and dissociation constants have been determined. The spin-labelled derivatives of ADP and ADPR exhibit a tighter binding than the corresponding NAD+ derivative. This may be attributed to the repulsion of the positively charged nicotinamide ring by an histidine side chain in the active center of the enzyme.

摘要

已合成了NAD+及其结构成分（即腺苷、腺嘌呤、AMP、ADP和ADPR）的自旋标记衍生物。研究了它们与猪心乳酸脱氢酶（L-乳酸：NAD+氧化还原酶，EC 1.1.1.27）的结合情况，并测定了解离常数。ADP和ADPR的自旋标记衍生物表现出比相应的NAD+衍生物更强的结合力。这可能归因于酶活性中心中组氨酸侧链对带正电荷的烟酰胺环的排斥作用。

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引用本文的文献

1
[Lactate dehydrogenase. An example of the development of modern enzymology].[乳酸脱氢酶。现代酶学发展的一个实例]
Naturwissenschaften. 1978 Aug;65(8):397-406. doi: 10.1007/BF00405363.

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