STRUCTURE AND CONTROL OF PHOSPHOFRUCTOKINASE FROM BACILLUS-STEAROTHERMOPHILUS

被引：187

作者：

EVANS, PR

HUDSON, PJ

机构：

[1] MRC, Laboratory of Molecular Biology, Cambridge, Hills Road

[2] Howard Florey Institute of Experimental Physiology and Medicine, University of Melbourne, Parkville

来源：

NATURE | 1979年 / 279卷 / 5713期

关键词：

D O I：

10.1038/279500a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The allosteric enzyme phosphofructokinase binds its substrate fructose-6-phosphate between two subunits of the tetramer, and allosteric effectors between another pair of subunits. The effector binding site accommodates both the activator and the inhibitor. The substrate cooperativity and allosteric control are mediated by these ligand bridges between subunits. © 1979 Nature Publishing Group.

引用

页码：500 / 504

页数：5

共 34 条

[31] TOPOLOGICAL COMPARISON OF ADENYL KINASE WITH OTHER PROTEINS [J].