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硫胺素焦磷酸结合机制及氨基嘧啶部分的功能。

Thiamin pyrophosphate binding mechanism and the function of the aminopyrimidine part.

作者信息

Schellenberger A

机构信息

Institute of Biochemistry (Enzymology Department), University of Halle-Wittenberg, Halle/Saale, Germany.

出版信息

J Nutr Sci Vitaminol (Tokyo). 1992;Spec No:392-6. doi: 10.3177/jnsv.38.special_392.

Abstract

Besides the pyrophosphate group, acting as the essential and primary binding function of TPP the N1-atom of the aminopyrimidine component functions as a second and also essential anchor to the protein component. Only if both of the contacts are formed the productive conformation of TPP within the active site of TPP enzymes is realized. A mechanism is proposed, which explains the results of our experiments with TPP-analogs.

摘要

除了焦磷酸基团作为硫胺素焦磷酸(TPP)的基本和主要结合功能外,氨基嘧啶组分的N1原子作为与蛋白质组分结合的第二个且同样重要的锚定点。只有当这两个接触点都形成时,TPP在TPP酶活性位点内的有效构象才能实现。我们提出了一种机制,用以解释我们用TPP类似物进行的实验结果。

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