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AF061: Prolyl oligopeptidase family
- Pfam domains
- PF00326: Prolyl oligopeptidase family
- PF00930: Dipeptidyl peptidase IV (DPP IV) N-terminal region
Biochemical properties
The members of this family of serine proteases belong to MEROPS family S9. It contains several subfamilies:
- Prolyl endopeptidases cleave peptide bonds on the C-terminal side of prolyl residues. They were identified in mammals and bacteria.
- Dipeptidyl peptidases IV remove N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
- Escherichia coli protease II (oligopeptidase B), which cleaves peptide bonds on the C-terminal side of lysyl and argininyl residues.
- Yeast vacuolar dipeptidyl aminopeptidases A and B.
- Acylamino acid-releasing enzymes (acyl peptide hydrolases), which catalyses the hydrolysis of the amino-terminal peptide bond of an N-acetylated protein.
Allergological significance
All allergens belonging to this family are dipeptidyl petidases. They were identified in several species of the dermatophytic fungus Trichophyton [1] and in bee and wasp venoms.
References
- Woodfolk JA, Wheatley LM, Piyasena RV, Benjamin DC, Platts-Mills TA.
Trichophyton antigens associated with IgE antibodies and delayed type hypersensitivity. Sequence homology to two families of serine proteinases.
J Biol Chem 1998, 273, 29489-96. [PubMed]
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