Prolyl endopeptidase and dipeptidyl peptidase IV are distantly related members of the same family of serine proteases.

L. Polgár, E. Szabo

Research output: Article

17 Citations (Scopus)

Abstract

Prolyl endopeptidase and dipeptidyl peptidase IV are serine proteases which cleave the peptide bonds at the carboxy group of proline residues. They do not show amino acid sequence homology with the known serine enzymes, but a possible relationship between them has not yet been examined. We have compared the amino acid sequences, and this revealed a distant evolutionary relationship between the two enzymes. Conserved segments were found mainly in the C-terminal region which also contained the catalytic residues. It is concluded that the C-terminal region is a protease domain which is attached to some noncatalytic structures.

Original languageEnglish
Pages (from-to)361-366
Number of pages6
JournalBiological Chemistry Hoppe-Seyler
Volume373
Issue number7
Publication statusPublished - júl. 1992

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prolyl oligopeptidase
Dipeptidyl Peptidase 4
Serine Proteases
Amino Acids
Amino Acid Sequence Homology
Enzymes
Proline
Serine
Amino Acid Sequence
Peptide Hydrolases
Peptides

ASJC Scopus subject areas

  • Biochemistry

Cite this

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abstract = "Prolyl endopeptidase and dipeptidyl peptidase IV are serine proteases which cleave the peptide bonds at the carboxy group of proline residues. They do not show amino acid sequence homology with the known serine enzymes, but a possible relationship between them has not yet been examined. We have compared the amino acid sequences, and this revealed a distant evolutionary relationship between the two enzymes. Conserved segments were found mainly in the C-terminal region which also contained the catalytic residues. It is concluded that the C-terminal region is a protease domain which is attached to some noncatalytic structures.",
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