磷酸二羟丙酮的膦酰甲基类似物与兔肌肉醛缩酶的相互作用。

Interaction of phosphonomethyl analog of dihydroxyacetone phosphate with rabbit muscle aldolase.

作者信息

Page P, Blonski C, Périé J

机构信息

Groupe de Chimie Organique Biologique, UMR CNRS 5623, Université Paul Sabatier, Bât. II R1, 118 route de Narbonne, 31062 Toulouse Cedex 4, France.

出版信息

Biochim Biophys Acta. 1998 Jul 28;1386(1):59-64. doi: 10.1016/s0167-4838(98)00061-2.

DOI:10.1016/s0167-4838(98)00061-2

PMID:9675245

Abstract

Aldolase presents the same binding affinity for dihydroxyacetone phosphate and its phosphonomethyl analog, but the partition coefficient between the intermediates from the Michaelis complex to the eneamine is different. The effects of the structural modification of the triose phosphate substrate on the interaction with rabbit muscle aldolase are discussed in connection with the mechanistic pathway and the three-dimensional structure of the enzyme.

摘要

醛缩酶对磷酸二羟丙酮及其膦酰甲基类似物具有相同的结合亲和力，但从米氏复合物到烯胺的中间体之间的分配系数不同。结合酶的作用机制途径和三维结构，讨论了磷酸丙糖底物的结构修饰对其与兔肌肉醛缩酶相互作用的影响。