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底物构象对α-芳基丙二酸酶促脱羧反应的影响

Effect of conformation of the substrate on enzymatic decarboxylation of alpha-arylmalonic acid.

作者信息

Miyamoto K, Ohta H, Osamura Y

机构信息

Department of Chemistry, Keio University, Yokohama, Japan.

出版信息

Bioorg Med Chem. 1994 Jun;2(6):469-75. doi: 10.1016/0968-0896(94)80016-2.

DOI:10.1016/0968-0896(94)80016-2
PMID:8000869
Abstract

The configuration and conformation of a compound are critical factors that determine whether it can be accepted by an enzyme as a substrate or not. We have examined enzyme-catalyzed decarboxylation of some alpha-substituted malonic acids and proposed that the syn-periplanar conformation is required for the substrates to be bound to the active site of the enzyme. Theoretical calculation of potential energy surfaces also supports the conclusion from experimental results.

摘要

化合物的构型和构象是决定其是否能被酶作为底物接受的关键因素。我们研究了一些α-取代丙二酸的酶催化脱羧反应,并提出底物要与酶的活性位点结合需要顺式-平面构象。势能面的理论计算也支持实验结果得出的结论。

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