Formation of the Michaelis complex without involvement of the prosthetic group dehydroalanine of histidine ammonialyase

被引：3

作者：

Langer, B ^{[1
]}

Starck, J ^{[1
]}

Langer, M ^{[1
]}

Retey, J ^{[1
]}

机构：

[1] UNIV KARLSRUHE,INST ORGAN CHEM,LEHRSTUHL BIOCHEM,DEPT BIOCHEM,D-76128 KARLSRUHE,GERMANY

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 1997年 / 7卷 / 08期

关键词：

D O I：

10.1016/S0960-894X(97)00158-3

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

The dehydroalanine-less S143G mutant of histidine ammonia-lyase was constructed and used for kinetic measurements with 5'-nitro-histidine as a substrate. The natural substrate histidine turned out to be a competitive inhibitor of the mutant enzyme and exhibited a K-i value which was similar to its K-m value with the wild-type enzyme. Thus the dehydroalanine prosthetic group does not play a role in formation of the Michaelis complex. (C) 1997 Elsevier Science Ltd.

引用

页码：1077 / 1082

页数：6

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