Abbott_1999_FEBS.Lett_458_278

Reference

Title : Two highly conserved glutamic acid residues in the predicted beta propeller domain of dipeptidyl peptidase IV are required for its enzyme activity - Abbott_1999_FEBS.Lett_458_278
Author(s) : Abbott CA , McCaughan GW , Gorrell MD
Ref : FEBS Letters , 458 :278 , 1999
Abstract : 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 beta 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.
ESTHER : Abbott_1999_FEBS.Lett_458_278
PubMedSearch : Abbott_1999_FEBS.Lett_458_278
PubMedID: 10570924

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Citations formats

Abbott CA, McCaughan GW, Gorrell MD (1999)
Two highly conserved glutamic acid residues in the predicted beta propeller domain of dipeptidyl peptidase IV are required for its enzyme activity
FEBS Letters 458 :278

Abbott CA, McCaughan GW, Gorrell MD (1999)
FEBS Letters 458 :278