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

Structure and control of phosphofructokinase from Bacillus stearothermophilus

P R Evans, P J Hudson

Structure and control of phosphofructokinase from Bacillus stearothermophilus

P R Evans et al. Nature. .

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.

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