The prolyl oligopeptidase family

Research output: Contribution to journalArticle

233 Citations (Scopus)

Abstract

A group of serine peptidases, the prolyl oligopeptidase family, cannot hydrolyze peptides containing more than about 30 residues. This group is unrelated to the classical trypsin and subtilisin families, and includes dipeptidyl peptidase IV, acylaminoacyl peptidase and oligopeptidase B, in addition to the prototype prolyl oligopeptidase. The recent crystal structure determination of prolyl oligopeptidase (80 kDa) has shown that the enzyme contains a peptidase domain with an α/β hydrolase fold, and its catalytic triad is covered by the central tunnel of an unusual seven-bladed β-propeller. This domain operates as a gating filter, excluding large, structured peptides from the active site. The binding mode of substrates and the catalytic mechanism differ from that of the classical serine peptidases in several features. The members of the family are important targets of drug design. Prolyl oligopeptidase is involved in amnesia, depression and blood pressure control, dipeptidyl peptidase IV in type 2 diabetes and oligopeptidase B in trypanosomiasis.

Original languageEnglish
Pages (from-to)349-362
Number of pages14
JournalCellular and Molecular Life Sciences
Volume59
Issue number2
DOIs
Publication statusPublished - 2002

Fingerprint

prolyl oligopeptidase
oligopeptidase B
Dipeptidyl Peptidase 4
Peptide Hydrolases
tripeptide aminopeptidase
Serine
Subtilisin
Peptides
Amnesia
Pressure control
Trypanosomiasis
Drug Design
Blood pressure
Hydrolases
Propellers
Medical problems
Trypsin
Type 2 Diabetes Mellitus
Catalytic Domain
Tunnels

Keywords

  • β-propeller structure
  • Acylaminoacyl peptidase
  • Catalytic mechanism
  • Dipeptidyl peptidase
  • Oligopeptidase B
  • Oligopeptidases
  • Prolyl oligopeptidase
  • Serine peptidases

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Cell Biology

Cite this

The prolyl oligopeptidase family. / Polgár, L.

In: Cellular and Molecular Life Sciences, Vol. 59, No. 2, 2002, p. 349-362.

Research output: Contribution to journalArticle

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