Peptide bond cis/trans isomerases: a biocatalysis perspective of conformational dynamics in proteins.

Cordelia Schiene-Fischer, Tobias Aumüller, Gunter Fischer

Max Planck Research Unit for Enzymology of Protein Folding, Halle/Saale, Germany. fischer@enzyme-halle.mpg.de

Topics in current chemistry 2013

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Peptide bond cis/trans isomerases (PCTIases) catalyze an intrinsically slow rotational motion taking part in the conformational dynamics of a protein backbone in all of its folding states. In this way, PCTIases assist other proteins to shape their functionally active structure. They have been associated with viral, bacterial, and parasitic infection, signal transduction, cell differentiation, altered metabolic activity, apoptosis, and many other physiological and pathophysiological processes. The need to understand, characterize, and control biochemical steps which contribute to the folding of proteins is a problem being addressed in many laboratories today. This review discusses the biochemical basis that the peptidyl prolyl cis/trans isomerase (PPIase) family of PCTIases uses for the control of bioactivity. Special emphasis is given to recent developments in the field of biocatalytic features of PPIases, the mechanism of catalysis, and enzyme inhibition.

Citation

Cordelia Schiene-Fischer, Tobias Aumüller, Gunter Fischer. Peptide bond cis/trans isomerases: a biocatalysis perspective of conformational dynamics in proteins. Topics in current chemistry. 2013;328:35-67