Two highly conserved glutamic acid residues in the predicted β propeller domain of dipeptidyl peptidase IV are required for its enzyme activity

FEBS Letters

Gorrell, Mark D¹  Abbott, Catherine A¹  McCaughan, Geoffrey W¹ 

[1]A.W. Morrow Gastroenterology and Liver Centre, Centenary Institute of Cell Biology and Cancer Medicine, Royal Prince Alfred Hospital and The University of Sydney, Locked Bag No. 6, Newton, N.S.W. 2042, Australia

关键词: Dipeptidyl peptidase IV;    Prolyl oligopeptidase;    β Propeller;    α/β Hydrolase fold;    DPP IV;    dipeptidyl peptidase IV;    POP;    prolyl oligopeptidase;    DPP;    dipeptidyl aminopeptidase;    FAP;    fibroblast activation protein;    mAb;    monoclonal antibody;    FITC;    fluorescein isothiocyanate;    ADA-FITC;    adenosine deaminase conjugated to FITC;    PE;    phycoerythrin;    HRP;    horseradish peroxidase;   

DOI  :  10.1016/S0014-5793(99)01166-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Dipeptidyl peptidase IV (DPP IV) is a member of the prolyl oligopeptidase family and modifies the biological activities of certain chemokines and neuropeptides by cleaving their N-terminal dipeptides. This paper reports the identification and possible significance of a novel conserved sequence motif Asp-Trp-(Val/Ile/Leu)-Tyr-Glu-Glu-Glu (DW(V/I/L)YEEE) in the predicted β propeller domain of the DPP IV-like gene family. Single amino acid point mutations in this motif identified two glutamates, at positions 205 and 206, as essential for the enzyme activity of human DPP IV. This observation suggests a novel role in proteolysis for residues of DPP IV distant from the Ser-Asp-His catalytic triad.

【 授权许可】

Unknown