InterPro domain: IPR034051

Tripeptidyl-peptidase II (MEROPS identifier S08.090) is a member of the peptidase S8 or subtilase family. Tripeptidyl-peptidase II removes tripeptides from the free N terminus of oligopeptides as well as having endoproteolytic activity. Some tripeptidyl-peptidases have been shown to cleave tripeptides and small peptides, e.g. angiotensin II and glucagon, while others are believed to be involved in MHC I processing [ 1 ].

Peptidases S8 (or subtilases serine endo- and exo-peptidase clan) have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values [ 2 , 3 , 4 , 5 ].

1. Tripeptidyl-peptidase II: a multi-purpose peptidase. Int. J. Biochem. Cell Biol. 37, 1933-7
2. Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteinases. Protein Eng. 4, 719-37
3. Structure and function of eukaryotic proprotein processing enzymes of the subtilisin family of serine proteases. Crit Rev Oncog 4, 115-36
4. Evolutionary families of peptidases. Biochem. J. 290 ( Pt 1), 205-18
5. Subtilases: the superfamily of subtilisin-like serine proteases. Protein Sci. 6, 501-23