PROSITE documentation PDOC00587

Prolyl oligopeptidase family serine active site




Description

The prolyl oligopeptidase family [1,2,3] consist of a number of evolutionary related peptidases whose catalytic activity seems to be provided by a charge relay system similar to that of the trypsin family of serine proteases, but which evolved by independent convergent evolution. The known members of this family are listed below.

  • Prolyl endopeptidase (EC 3.4.21.26) (PE) (also called post-proline cleaving enzyme). PE is an enzyme that cleaves peptide bonds on the C-terminal side of prolyl residues. The sequence of PE has been obtained from a mammalian species (pig) and from bacteria (Flavobacterium meningosepticum and Aeromonas hydrophila); there is a high degree of sequence conservation between these sequences.
  • Escherichia coli protease II (EC 3.4.21.83) (oligopeptidase B) (gene prtB) which cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues.
  • Dipeptidyl peptidase IV (EC 3.4.14.5) (DPP IV). DPP IV is an enzyme that removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
  • Yeast vacuolar dipeptidyl aminopeptidase A (DPAP A) (gene: STE13) which is responsible for the proteolytic maturation of the α-factor precursor.
  • Yeast vacuolar dipeptidyl aminopeptidase B (DPAP B) (gene: DAP2).
  • Acylamino-acid-releasing enzyme (EC 3.4.19.1) (acyl-peptide hydrolase). This enzyme catalyzes the hydrolysis of the amino-terminal peptide bond of an N-acetylated protein to generate a N-acetylated amino acid and a protein with a free amino-terminus.

A conserved serine residue has experimentally been shown (in E.coli protease II as well as in pig and bacterial PE) to be necessary for the catalytic mechanism. This serine, which is part of the catalytic triad (Ser, His, Asp), is generally located about 150 residues away from the C-terminal extremity of these enzymes (which are all proteins that contains about 700 to 800 amino acids).

Note:

These proteins belong to families S9A/S9B/S9C in the classification of peptidases [4,E1].

Last update:

November 1997 / Text revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

PRO_ENDOPEP_SER, PS00708; Prolyl endopeptidase family serine active site  (PATTERN)


References

1AuthorsRawlings N.D., Polgar L., Barrett A.J.
TitleA new family of serine-type peptidases related to prolyl oligopeptidase.
SourceBiochem. J. 279:907-908(1991).
PubMed ID1953688

2AuthorsBarrett A.J., Rawlings N.D.
TitleOligopeptidases, and the emergence of the prolyl oligopeptidase family.
SourceBiol. Chem. Hoppe-Seyler 373:353-360(1992).
PubMed ID1515061

3AuthorsPolgar L., Szabo E.
TitleProlyl endopeptidase and dipeptidyl peptidase IV are distantly related members of the same family of serine proteases.
SourceBiol. Chem. Hoppe-Seyler 373:361-366(1992).
PubMed ID1355343

4AuthorsRawlings N.D., Barrett A.J.
TitleFamilies of serine peptidases.
SourceMethods Enzymol. 244:19-61(1994).
PubMed ID7845208

E1Sourcehttp://www.uniprot.org/docs/peptidas



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)