PMID- 10570924
OWN - NLM
STAT- MEDLINE
DCOM- 20000229
LR  - 20201208
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 458
IP  - 3
DP  - 1999 Sep 24
TI  - Two highly conserved glutamic acid residues in the predicted beta propeller
      domain of dipeptidyl peptidase IV are required for its enzyme activity.
PG  - 278-84
AB  - 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.
FAU - Abbott, C A
AU  - Abbott CA
AD  - A.W. Morrow Gastroenterology and Liver Centre, Centenary Institute of Cell
      Biology and Cancer Medicine, Royal Prince Alfred Hospital and the University of
      Sydney, Newton, NSW, Australia. c.abbott@centenary.usyd.edu.au
FAU - McCaughan, G W
AU  - McCaughan GW
FAU - Gorrell, M D
AU  - Gorrell MD
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 3KX376GY7L (Glutamic Acid)
RN  - EC 3.4.14.5 (Dipeptidyl Peptidase 4)
RN  - EC 3.4.21.- (Serine Endopeptidases)
RN  - EC 3.4.21.26 (PREPL protein, human)
RN  - EC 3.4.21.26 (Prolyl Oligopeptidases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - COS Cells
MH  - Conserved Sequence
MH  - Dipeptidyl Peptidase 4/*chemistry/genetics
MH  - Flow Cytometry
MH  - Fluorescent Antibody Technique
MH  - Glutamic Acid/*chemistry/genetics
MH  - Humans
MH  - Kinetics
MH  - Molecular Sequence Data
MH  - Point Mutation
MH  - Prolyl Oligopeptidases
MH  - Sequence Alignment
MH  - Serine Endopeptidases/chemistry/genetics
MH  - Substrate Specificity
MH  - Transfection
EDAT- 1999/11/26 09:00
MHDA- 2000/03/04 09:00
CRDT- 1999/11/26 09:00
PHST- 1999/11/26 09:00 [pubmed]
PHST- 2000/03/04 09:00 [medline]
PHST- 1999/11/26 09:00 [entrez]
AID - S0014-5793(99)01166-7 [pii]
AID - 10.1016/s0014-5793(99)01166-7 [doi]
PST - ppublish
SO  - FEBS Lett. 1999 Sep 24;458(3):278-84. doi: 10.1016/s0014-5793(99)01166-7.