Dipeptidyl Peptidase IV

Supporting information

Dipeptidyl Peptidase IV (DPP-IV) (also known as CD26) is a ubiquitous, membrane-bound enzyme that has roles in nutrition, metabolism, the immune and endocrine systems, bone marrow mobilization, cancer growth and cell adhesion.

DDP-IV catalyzes the hydrolysis of N-terminal dipeptides from polypeptides with proline or alanine in the penultimate position. This enzyme has many natural substrates including GLP-1, GIP, PACAP 38, NPY and GRP. DPP-IV exists as a homodimer and each monomer consists of two domains; an α/β hydrolase domain and an eight-blade β-propeller domain. DDP-IV binds to, but does not cleave, adenosine deaminase, kidney Na+/H+ ion exchanger and fibronectin, which localizes these molecules to the cell surface. A soluble form of DDP-IV does also exist, although it is only known to function in relation to T-cell proliferation. The human gene encoding DPP-IV is localized to chromosome 2q24.2.

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Species Gene Symbol Gene Accession No. Protein Accession No.
Human DPP4 NM_001935 P27487
Mouse Dpp4 NM_010074 P28843
Rat Dpp4 NM_012789 P14740

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