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Structure and control of phosphofructokinase from Bacillus stearothermophilus

Nature volume 279, pages 500–504 (1979)Cite this article

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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Author notes

  1. P. J. Hudson

    Present address: Howard Florey Institute of Experimental Physiology and Medicine, University of Melbourne, Parkville, Victoria, 3152, Australia

Authors and Affiliations

  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge, UK

    P. R. Evans & P. J. Hudson

Authors
  1. P. R. Evans
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  2. P. J. Hudson
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Evans, P., Hudson, P. Structure and control of phosphofructokinase from Bacillus stearothermophilus. Nature 279, 500–504 (1979). https://doi.org/10.1038/279500a0

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