AF061: Prolyl oligopeptidase family
- Pfam domains
- PF00326: Prolyl oligopeptidase family
- PF00930: Dipeptidyl peptidase IV (DPP IV) N-terminal region
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.
All allergens belonging to this family are dipeptidyl petidases. They were identified in several species of the dermatophytic fungus Trichophyton  and in bee and wasp venoms.
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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