Peptidylprolyl isomerase C

Peptidylprolyl isomerase C refers to an enzyme that catalyzes the cis-trans isomerization of peptide bonds at proline residues in polypeptides, a key step in protein folding and regulation of protein function[2][4][5]. These enzymes, collectively known as peptidyl-prolyl cis-trans isomerases (PPIases), are found in all domains of life and fall into three main families: cyclophilins, FK506-binding proteins, and parvulins[5]. Cyclophilin C (PPIC), sometimes called peptidylprolyl isomerase C, is a member of the cyclophilin family and has been implicated in immune regulation because it binds the immunosuppressive drug cyclosporin A[5]. PPIases, including Pin1 and related enzymes, have roles in cell cycle progression, gene regulation, and disease states such as cancer, viral infection, and neurodegeneration[1][5]. The designation "peptidylprolyl isomerase C" is specific but may be ambiguous, as most data and therapeutic targeting efforts focus on distinct isoforms (e.g., Pin1, cyclophilin A/B/C), so caution is warranted in mapping literature references[5].

Other names

PPIase Ccyclophilin CPPIC

Inhibition by binding to active site (e.g., cyclosporin A inhibits cyclophilins, affecting isomerase activity and downstream pathways)