Allostery in enzyme catalysis

George P Lisi; J Patrick Loria

doi:10.1016/j.sbi.2017.08.002

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.

Authors

George P Lisi¹, J Patrick Loria²

Affiliations

¹ Department of Chemistry, Yale University, New Haven, CT, USA. Electronic address: [email protected].
² Department of Chemistry, Yale University, New Haven, CT, USA; Department of Molecular Biophysics & Biochemistry, Yale University, New Haven, CT, USA. Electronic address: [email protected].

PMID: 28865247
DOI: 10.1016/j.sbi.2017.08.002

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