Home | Contact

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).

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

November 1997 / Text revised.

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

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

Consensus pattern: D-x(3)-A-x(3)-[LIVMFYW]-x(14)-G-x-S-x-G-G-[LIVMFYW](2) S is the active site residue Sequences known to belong to this class detected by the pattern: ALL, except for yeast DPAP A Other sequence(s) detected in Swiss-Prot: NONE.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00708 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00708 • Scan Swiss-Prot/TrEMBL entries against PS00708 • view ligand binding statistics

Matching PDB structures: 1E5T 1H2W 1H2X 1H2Y ... [ALL]

1	Authors	Rawlings N.D., Polgar L., Barrett A.J.
	Title	A new family of serine-type peptidases related to prolyl oligopeptidase.
	Source	Biochem. J. 279:907-908(1991).
	PubMed ID	1953688

2	Authors	Barrett A.J., Rawlings N.D.
	Title	Oligopeptidases, and the emergence of the prolyl oligopeptidase family.
	Source	Biol. Chem. Hoppe-Seyler 373:353-360(1992).
	PubMed ID	1515061

3	Authors	Polgar L., Szabo E.
	Title	Prolyl endopeptidase and dipeptidyl peptidase IV are distantly related members of the same family of serine proteases.
	Source	Biol. Chem. Hoppe-Seyler 373:361-366(1992).
	PubMed ID	1355343

4	Authors	Rawlings N.D., Barrett A.J.
	Title	Families of serine peptidases.
	Source	Methods Enzymol. 244:19-61(1994).
	PubMed ID	7845208

E1
Source	http://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.


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

SIB Swiss Institute of Bioinformatics | Disclaimer