Molecular cloning and sequence analysis of human dipeptidyl peptidase IV, a serine proteinase on the cell surface.
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Misumi Y, Hayashi Y, Arakawa F, Ikehara Y
Molecular cloning and sequence analysis of human dipeptidyl peptidase IV, a serine proteinase on the cell surface.
Biochim Biophys Acta. 1992 Jul 15;1131(3):333-6.
- PubMed ID
- 1352704 [ View in PubMed]
- Abstract
The cDNA coding for the human dipeptidyl peptidase IV (DPPIV) has been isolated and sequenced. The nucleotide sequence (3465 bp) of the cDNA contains an open reading frame encoding a polypeptide comprising 766 amino acids, one residue less than those of rat DPPIV. The predicted amino acid sequence exhibits 84.9% identity to that of the rat enzyme, and contains nine potential N-linked glycosylation sites, one site more than those in the rat enzyme. A putative catalytic triad for serine proteinases, serine, aspartic acid and histidine, are found in a completely conserved COOH-terminal region (positions 625-752).