Multidomain Peptidyl Prolyl cis/trans Isomerases

Area of Science:

• Enzymology
• Molecular Biology
• Cellular Biology

Background:

• Peptidyl prolyl cis/trans isomerases (PPIases) are enzymes that catalyze the rate-limiting cis/trans isomerization of peptide bonds preceding proline residues, crucial for protein folding.
• These enzymes are implicated in diverse cellular processes, including signal transduction, differentiation, apoptosis, and host-pathogen interactions.

Purpose of the Study:

• This review examines the biochemical and functional characteristics of multidomain PPIases.
• It focuses on PPIase members that incorporate additional protein domains with distinct biochemical functions.

Main Methods:

• Review of existing literature on multidomain PPIases.
• Analysis of the role of accessory domains in PPIase function.

Main Results:

• Multidomain PPIases exhibit versatile domain architectures, influencing enzyme specificity and subcellular localization.
• Accessory domains provide an additional regulatory layer for prolyl isomerization catalysis, impacting specific client proteins.

Conclusions:

• The domain composition of multidomain PPIases is critical for precise control of enzymatic activity and cellular targeting.
• Understanding these regulatory mechanisms enhances insights into PPIase physiological roles and potential as therapeutic targets.