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Current Medicinal Chemistry

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ISSN (Print): 0929-8673
ISSN (Online): 1875-533X

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Review Article

Research Progress on Dipeptidyl Peptidase Family: Structure, Function and Xenobiotic Metabolism

Author(s): Xing-Kai Qian, Jing Zhang, Xiao-Dong Li, Pei-Fang Song and Li-Wei Zou*

Volume 29, Issue 12, 2022

Published on: 11 January, 2022

Page: [2167 - 2188] Pages: 22

DOI: 10.2174/0929867328666210915103431

Price: $65

Abstract

Prolyl-specific peptidases or proteases, including Dipeptidyl Peptidase 2, 4, 6, 8, 9, 10, Fibroblast Activation Protein, prolyl endopeptidase, and prolyl carboxypeptidase, belong to the dipeptidyl peptidase family. In human physiology and anatomy, they have homology amino acid sequences and similarities in the structure; however, they have distinct functions and play different roles. Some of them also play important roles in the metabolism of drugs containing endogenous peptides, xenobiotics containing peptides, and exogenous peptides. The major functions of these peptidases in both the metabolism of human health and bioactive peptides are of significant importance in the development of effective inhibitors to control the metabolism of endogenous bioactive peptides. The structural characteristics, distribution of tissue, endogenous substrates, and biological functions were summarized in this review. Furthermore, the xenobiotics metabolism of the dipeptidyl peptidase family is illustrated. All the evidence and information summarized in this review would be very useful for researchers to extend the understanding of the proteins of these families and offer advice and assistance in physiology and pathology studies.

Keywords: Dipeptidyl peptidase family, metabolism, detection methods, inhibitor, prolyl carboxypeptidase, FAP.

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