Summary for peptidase S08.090: tripeptidyl-peptidase II

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Structure Literature Human EST Mouse EST Substrates Inhibitors


MEROPS Nametripeptidyl-peptidase II
Other namesAtSBT6.2 (Arabidopsis thaliana), cholecystokinin 8-inactivating peptidase, multicorn peptidase (Schizosaccharomyces pombe), TPP II, TPP2 g.p. (Homo sapiens), tripeptidyl aminopeptidase, tripeptidyl peptidase
Domain architecture
MEROPS Classification
Classification Clan SB >> Subclan (none) >> Family S8 >> Subfamily A >> S08.090
Holotypetripeptidyl-peptidase II (Drosophila melanogaster), Uniprot accession Q9V6K1 (peptidase unit: 92-609), MERNUM MER0011484
History Identifier created: Handbook of Proteolytic Enzymes (1998) Academic Press, London.
Catalytic typeSerine
PeplistIncluded in the Peplist with identifier PL00365
NC-IUBMBSubclass 3.4 (Peptidases) >> Sub-subclass 3.4.14 (Dipeptidyl-peptidase and tripeptidyl-peptidases) >> Peptidase
EnzymologyBRENDA database
Activity statushuman: active (Tomkinson, 2004)
mouse: active (Tomkinson et al., 1997)
InhibitorsButabindide is regarded as a highly specific inhibitor (Rose et al., 1996).
PhysiologyContributes to cytosolic degradation of oligopeptides, and to the late stages of processing of antigenic peptides for the MHC class I system (Levy et al., 2002).
Pharmaceutical relevanceSince tripeptidyl-peptidase II is responsible for much of the degradation of cholecystokinin-8, there is interest in inhibitors as drugs (Breslin et al., 2003).
Other databases TREEFAM