Dipeptidyl Peptidase III: Physiological Role, Monitoring and Inhibition
A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Macromolecular Chemistry".
Deadline for manuscript submissions: closed (31 October 2022) | Viewed by 6660
Special Issue Editor
Interests: protein interactions; medicinal chemistry; chemical biology; computational chemistry; reaction mechanisms; enzymology; drug design; thermodynamics
Special Issue Information
Dear Colleagues,
Dipeptidyl peptidase III (DPP III; EC 3.4.14.4) is a zinc peptidase of the M49 family and the only metalloenzyme among the dipeptidyl peptidases. It is defined by five evolutionarily conserved regions, including two characteristic motifs, HEXXGH and EEXR(K) AE (D), that are critical for zinc binding and catalytic activity. This cytosolic enzyme, widely distributed in various species and tissues, cleaves dipeptides from the unsubstituted amino end of its substrate. DPP III shows a marked affinity for several bioactive peptides (angiotensins II, III, IV and opioid peptides) as well as flavonoids and various peptidomimetics, many of which contain a large aromatic moiety. The broad substrate specificity of human DPP III may be due to the high flexibility of its 3D structure and the plasticity of its ligand-binding site. In addition to its role in the final stages of protein turnover, it is also involved in a number of physiological and pathophysiological processes, such as defense against oxidative stress, apoptosis, and inflammation, but the details of its biological effects are still unknown. Moreover, the increased amount and activity of DPP III compared to normal tissues suggest that it is involved in the development of some cancers. Therefore, the new search for effective inhibitors and fluorescent ligands of human DPP III would be of great importance to define its physiological role and therapeutic potential.
This Special Issue will focus on new findings revealing these biological functions and researchers are invited to contribute with their high quality research articles from all research areas to elucidate the physiological role of DPP III and search for its inhibitors and ligands.
Prof. Dr. Sanja Tomić
Guest Editor
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Keywords
- dipeptidyl peptidase III
- metalloenzyme
- inhibition
- peptides
- oxidative stress
- fluorescent probes
- enzymatic mechanism
- biopeptides
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