Encyclopedia of Signaling Molecules

Living Edition
| Editors: Sangdun Choi

Dipeptidyl Peptidase 4

Living reference work entry
DOI: https://doi.org/10.1007/978-1-4614-6438-9_101580-1


Historical Background

Nature has evolved a number of regulatory, neuronal, and immune peptides with a proline residue at the penultimate position determining their structural conformation and biological activity. Generally, the proline peptide bonds are resistant to proteolytic cleavage, yet an exclusive number of postproline-specific peptidases have emerged to regulate these peptides. The best-characterized one is dipeptidyl peptidase 4 (DPP4), though additional functional homologues of DPP4-like enzymes have been discovered, some structurally related, others without any structural homology. Since DPP4 is involved in glucose homeostasis and immune response, it is of medical and pharmaceutical interest to distinguish between these enzymes (Klemann et al. 2016; Lambeir et al. 2003; Wagner et al. 2016b).

DPP4 [EC] was first discovered in 1966 by Hopsu-Havu and Glenner and denoted with glycyl-prolyl-β-naphtylamidase. Other names include...


Natural Killer Cell DPP4 Inhibitor Adenosine Deaminase Dipeptidyl Peptidase Gastrin Release Peptide 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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© Springer Science+Business Media LLC 2016

Authors and Affiliations

  1. 1.Deutschsprachige Selbsthilfegruppe für Alkaptonurie e.VStuttgartGermany