Allostery in enzyme catalysis

Curr Opin Struct Biol. 2017 Dec:47:123-130. doi: 10.1016/j.sbi.2017.08.002. Epub 2017 Sep 1.

Abstract

Modern interpretations of allostery typically rely on conformational ensembles to describe enzyme function. Conformational motions controlling these ensembles are often stimulated or quenched by allosteric effectors, and are critical to optimizing ligand binding pockets and enzyme architectures. Thus, enzymes rely on dynamic allosteric pathways that transmit long-range binding information to control catalysis. In this review, we provide a brief discussion of the ever-expanding principles of allosteric regulation in enzyme catalysis and highlight in-depth studies of three enzymes that have contributed to the paradigms of dynamic allostery.

Publication types

  • Review

MeSH terms

  • Allosteric Regulation*
  • Allosteric Site
  • Aminohydrolases / chemistry
  • Aminohydrolases / metabolism
  • Catalysis
  • Catalytic Domain
  • Cyclic AMP-Dependent Protein Kinase Catalytic Subunits / chemistry
  • Cyclic AMP-Dependent Protein Kinase Catalytic Subunits / metabolism
  • Enzymes / chemistry*
  • Enzymes / metabolism*
  • Models, Molecular
  • Protein Binding
  • Protein Conformation*
  • Protein Interaction Domains and Motifs
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1 / chemistry
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1 / metabolism
  • Structure-Activity Relationship

Substances

  • Enzymes
  • Cyclic AMP-Dependent Protein Kinase Catalytic Subunits
  • Protein Tyrosine Phosphatase, Non-Receptor Type 1
  • imidazole glycerol phosphate synthase
  • Aminohydrolases