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Enzymatic Activity and Protein Interactions in Alpha/Beta Hydrolase Fold Proteins: Moonlighting Versus Promiscuity

[ Vol. 19 , Issue. 2 ]

Author(s):

Pascale Marchot and Arnaud Chatonnet   Pages 132 - 143 ( 12 )

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.

Keywords:

Alpha/beta hydrolase fold, catalytic site, cholinesterase, enzyme, partnership, structure-function relationship, Genes, transporters, receptors, chaperones

Affiliation:

(PM) Centre de Recherche en Neurobiologie-Neurophysiologie de Marseille (CRN2M), CNRS/Universites Aix-Marseille UMR-6231, Institut Federatif de Recherche Jean Roche, Faculte de Medecine-Secteur Nord, F-13344 Marseille, France.



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