Enzymatic activity and protein interactions in alpha/beta hydrolase fold proteins: moonlighting versus promiscuity

Protein Pept Lett. 2012 Feb;19(2):132-43. doi: 10.2174/092986612799080284.

Abstract

Genes coding for members of the alpha/beta hydrolase fold superfamily of proteins are present in all known genomes. Although there is no common and essential function performed by these proteins shared in all living organisms, this fold has been used for a number of diverse functions. The ancestry of both enzymatic and protein-protein interaction capability of this structural scaffold made it an important tinkering tool kit for protein function evolution. Recently, enzymes known since a long time have been found to have a second function in acting promiscuously on alternative substrates, or to be true moonlighting proteins acting also as transporters, receptors, chaperones… The reverse situation has been encountered for adhesion proteins shown to be enzymes. This review, while not exhaustive, surveys some of the best-known examples of multiple functions in alpha/beta hydrolase fold proteins.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Binding, Competitive / physiology
  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism
  • Carrier Proteins / physiology
  • Enzyme Activation / physiology
  • Humans
  • Hydrolases / chemistry*
  • Hydrolases / genetics
  • Hydrolases / metabolism*
  • Hydrolases / physiology
  • Models, Biological
  • Models, Molecular
  • Multigene Family / genetics
  • Multigene Family / physiology
  • Protein Binding / physiology
  • Protein Interaction Mapping* / methods
  • Structural Homology, Protein
  • Structure-Activity Relationship
  • Substrate Specificity

Substances

  • Carrier Proteins
  • Hydrolases