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Peptide Bond cis/trans Isomerases: A Biocatalysis Perspective of Conformational Dynamics in Proteins

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Molecular Chaperones

Part of the book series: Topics in Current Chemistry ((TOPCURRCHEM,volume 328))

Abstract

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.

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Abbreviations

APIase:

Secondary amide peptide bond cis/trans isomerase

CsA:

Cyclosporine A

CypA:

Cyclophilin A; cyclophilin18

NMR:

Nuclear magnetic resonance

PCTI:

Peptide bond cis/trans isomerization

PCTIase:

Peptide bond cis/trans isomerase

PPIase:

Peptidyl prolyl cis/trans isomerase

SFA:

Sanglifehrin A

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Authors and Affiliations

  1. Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120, Halle/Saale, Germany

    Cordelia Schiene-Fischer, Tobias Aumüller & Gunter Fischer

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  1. Cordelia Schiene-Fischer
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  2. Tobias Aumüller
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  3. Gunter Fischer
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Correspondence to Cordelia Schiene-Fischer .

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  1. Dept. Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, United Kingdom

    Sophie Jackson

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Schiene-Fischer, C., Aumüller, T., Fischer, G. (2011). Peptide Bond cis/trans Isomerases: A Biocatalysis Perspective of Conformational Dynamics in Proteins. In: Jackson, S. (eds) Molecular Chaperones. Topics in Current Chemistry, vol 328. Springer, Berlin, Heidelberg. https://doi.org/10.1007/128_2011_151

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