THREONINE-SENSITIVE HOMOSERINE DEHYDROGENASE AND ASPARTOKINASE ACTIVITIES OF ESCHERICHIA-COLI K12 - A STUDY OF ALLOSTERIC EQUILIBRIUM

被引：53

作者：

JANIN, J

COHEN, GN

机构：

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1969年 / 11卷 / 03期

关键词：

D O I：

10.1111/j.1432-1033.1969.tb00804.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Aspartokinase I‐homoserine dehydrogeanase I is an allosteric protein with six subunits. Conformation changes upon addition of a substrate, l‐aspartate, and of an activator, K+, or an inhibitor, l‐threonine, are demonstrated by a study of the ultraviolet absorption and of the fluorescence emission of the protein. The effects of the ligands are compatible with a two‐state model and a three‐by‐three concerted transition of the subunits from the inactive, threonine binding conformation, to the active conformation binding aspartate and the potassium ions. Copyright © 1969, Wiley Blackwell. All rights reserved

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页码：520 / &

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