THEORETICAL-ANALYSIS OF KINETIC-BEHAVIOR OF HYSTERETIC ALLOSTERIC ENZYMES .1. KINETIC MANIFESTATIONS OF SLOW CONFORMATIONAL CHANGE OF AN OLIGOMERIC ENZYME IN MONOD, WYMAN AND CHANGEUX MODEL

被引：49

作者：

KURGANOV, BI ^{[1
]}

DOROZHKO, AI ^{[1
]}

KAGAN, ZS ^{[1
]}

YAKOVLEV, VA ^{[1
]}

机构：

[1] ALL UNION VITAMIN RES INST, MOSCOW, USSR

来源：

JOURNAL OF THEORETICAL BIOLOGY | 1976年 / 60卷 / 02期

关键词：

D O I：

10.1016/0022-5193(76)90059-X

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The curves of the time (t) dependent product (Pr) accumulation for Monod, Wyman and Changeux model (1965), where the rate of installation of equilibrium between 2 conformational states of oligomeric enzyme (R .dblarw. T) is comparable to that of enzymatic process, are theoretically analyzed. It is assumed that the complexes of R and T forms are in rapid equilibrium with the free components. The character of the effective rate constant of conformational transition R .dblarw. T and the value of .tau. (where .tau. is the intercept of the linear part of the kinetic curve of [Pr] vs. t with the time axis) vs. the substrate concentration is analyzed. It is also shown that slow conformational transition R .dblarw. T can be manifested by an unusual shape for Monod et al. model plots of initial velocity of the enzyme reaction vs. the substrate concentration. These curves can clearly display expressed inflection points and Hill''s cooperativity coefficient < 1.

引用

页码：247 / 269

页数：23

共 51 条

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