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嗜热脂肪芽孢杆菌磷酸果糖激酶的结构与调控

Structure and control of phosphofructokinase from Bacillus stearothermophilus.

作者信息

Evans P R, Hudson P J

出版信息

Nature. 1979 Jun 7;279(5713):500-4. doi: 10.1038/279500a0.

DOI:10.1038/279500a0
PMID:156307
Abstract

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.

摘要

变构酶磷酸果糖激酶在四聚体的两个亚基之间结合其底物6-磷酸果糖,而变构效应物则结合在另一对亚基之间。效应物结合位点既能容纳激活剂,也能容纳抑制剂。底物协同性和变构调控是由亚基之间的这些配体桥介导的。

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