An active-site mutation (Gly633 .fwdarw. Arg) of dipeptidyl peptidase IV causes its retention and rapid degradation in the endoplasmic reticulum

Biochemistry ◽  
1992 ◽  
Vol 31 (47) ◽  
pp. 11921-11927 ◽  
Author(s):  
Emiko Tsuji ◽  
Yoshio Misumi ◽  
Toshiyuki Fujiwara ◽  
Noboru Takami ◽  
Shigenori Ogata ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Active Site ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Site Mutation ◽  
Rapid Degradation

scholarly journals Crystal Structures of HIV-1 Tat-derived Nonapeptides Tat-(1–9) and Trp2-Tat-(1–9) Bound to the Active Site of Dipeptidyl-peptidase IV (CD26)

2005 ◽  
Vol 280 (15) ◽  
pp. 14911-14917 ◽  
Author(s):  
Wilhelm Andreas Weihofen ◽  
Jianguo Liu ◽  
Werner Reutter ◽  
Wolfram Saenger ◽  
Hua Fan
Keyword(s):  
Crystal Structures ◽  
Active Site ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Hiv 1

A Dipeptidyl Peptidase IV Inhibitory Peptide Relieves Palmitic Acid-Induced Endoplasmic Reticulum Stress in HepG2 Cells Independently of Inhibiting Dipeptidyl Peptidase IV Activity

2021 ◽  
Author(s):  
Ritian Jin ◽  
Haowei Ren ◽  
Minhe Liao ◽  
Jiaqi Shang ◽  
Dangfeng Wang ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
Palmitic Acid ◽  
Er Stress ◽  
Hepg2 Cells ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Inhibitory Peptide ◽  
Dpp Iv

The peptide VLATSGPG (VLA) is known to inhibit dipeptidyl peptidase IV (DPP-IV), although its mechanism in relieving endoplasmic reticulum (ER) stress is unclear. In this study, we found that treating...

A comparative study of the binding modes of recently launched dipeptidyl peptidase IV inhibitors in the active site

2013 ◽  
Vol 434 (2) ◽  
pp. 191-196 ◽  
Author(s):  
Mika Nabeno ◽  
Fumihiko Akahoshi ◽  
Hiroyuki Kishida ◽  
Ikuko Miyaguchi ◽  
Yoshihito Tanaka ◽  
...  
Keyword(s):  
Comparative Study ◽  
Active Site ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Binding Modes ◽  
Dipeptidyl Peptidase Iv Inhibitors

scholarly journals The Binding Site of Human Adenosine Deaminase for Cd26/Dipeptidyl Peptidase IV

2000 ◽  
Vol 192 (9) ◽  
pp. 1223-1236 ◽  
Author(s):  
Eva Richard ◽  
Francisco X. Arredondo-Vega ◽  
Ines Santisteban ◽  
Susan J. Kelly ◽  
Dhavalkumar D. Patel ◽  
...  
Keyword(s):  
Adenosine Deaminase ◽  
Severe Combined Immunodeficiency ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Site Mutation ◽  
Extracellular Adenosine ◽  
Human T Cell ◽  
Helical Segment ◽  
Cell Membrane Protein ◽  
Human T Cell Line

Human, but not murine, adenosine deaminase (ADA) forms a complex with the cell membrane protein CD26/dipeptidyl peptidase IV. CD26-bound ADA has been postulated to regulate extracellular adenosine levels and to modulate the costimulatory function of CD26 on T lymphocytes. Absence of ADA–CD26 binding has been implicated in causing severe combined immunodeficiency due to ADA deficiency. Using human–mouse ADA hybrids and ADA point mutants, we have localized the amino acids critical for CD26 binding to the helical segment 126–143. Arg142 in human ADA and Gln142 in mouse ADA largely determine the capacity to bind CD26. Recombinant human ADA bearing the R142Q mutation had normal catalytic activity per molecule, but markedly impaired binding to a CD26+ ADA-deficient human T cell line. Reduced CD26 binding was also found with ADA from red cells and T cells of a healthy individual whose only expressed ADA has the R142Q mutation. Conversely, ADA with the E217K active site mutation, the only ADA expressed by a severely immunodeficient patient, showed normal CD26 binding. These findings argue that ADA binding to CD26 is not essential for immune function in humans.

Discovery of non-covalent dipeptidyl peptidase IV inhibitors which induce a conformational change in the active site

2007 ◽  
Vol 17 (6) ◽  
pp. 1765-1768 ◽  
Author(s):  
Scott M. Sheehan ◽  
Hans-Juergen Mest ◽  
Brian M. Watson ◽  
Valentine J. Klimkowski ◽  
David E. Timm ◽  
...  
Keyword(s):  
Conformational Change ◽  
Active Site ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Dipeptidyl Peptidase Iv Inhibitors

Identification of the active site residues in dipeptidyl peptidase IV by affinity labeling and site-directed mutagenesis

Biochemistry ◽  
1992 ◽  
Vol 31 (9) ◽  
pp. 2582-2587 ◽  
Author(s):  
Shigenori Ogata ◽  
Yoshio Misumi ◽  
Emiko Tsuji ◽  
Noboru Takami ◽  
Kimimitsu Oda ◽  
...  
Keyword(s):  
Active Site ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Site Directed Mutagenesis ◽  
Affinity Labeling ◽  
Directed Mutagenesis ◽  
Active Site Residues
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