Tripeptidyl peptidases

An exopeptidase that sequentially releases a dipeptide from the N-terminus of a protein or peptide. Dipeptidy 1-peptidases are included in Enzyme Nomenclature subsubclass 3.4.14 along with tripeptidyl-peptidases. 

Peptide scaffold-based design strategies thrombin and tripeptidyl peptidase II... 

The recent discovery of peptidomimetic inhibitors of the serine protease TTP-II (tripeptidyl peptidase-II) further illustrates the peptide scaffold-based design approach [72]. Specifically, relative to a known TTP-... 

Lukacs Z, Santavuori P, Keil A, Steinfeld R, Kohlschiitter A (2003) Rapid and simple assay for the determination of tripeptidyl peptidase and palmitoyl protein thioesterase activities in dried blood spots. Clin Chem 49 509-511... 

Rawlings, N. D., and Barrett, A. J. (1999). Tripeptidyl-peptidase I is apparently the CLN2 protein absent in classical late-infantile neuronal ceroid lipofuscinosis. Biochim. Biophys. Acta, 1429, 496-500. 

Ezaki, J., Takeda-Ezaki, M., Oda, K., and Kominami, E. (2000). Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2 protein which is deficient in classical late infatile neuronal ceroid lipofuscinosis. Biochem. Biophys. Res.Commun., 268, 904-908. 

Lin, L., Sohar, I., Lackland, H., and Lobel, P. (2001). The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH., J. 

Tartar, A., and Boucias, D. G. (2004). A pilot-scale expressed sequence tag analysis of Beauveria bassiana gene expression reveals a tripeptidyl peptidase that is differentially expressed invivo.Mycopathologia, 158, 201-209. 

Du/tripeptidyl-peptidases Peptidyl-dipeptidases Serine carboxypeptidases MetaUocarboxypeptidases Cysteine carboxypeptidases Omega peptidases Serine endopeptidases Cysteine endopeptidases Aspartic endopeptidases MetaUoendopeptidases Threonine endopeptidases Other endopeptidases... 

The condition is caused by deficiencies of palmitoyl protein thioesterase 1 (PPTl) (or tripeptidyl peptidase 1 (TPPl) and possibly other enzymes resulting in the same clinical presentation of NCL (for Aeural Ceroid Lipofuscinose)). PPTl cleaves long-chain fatty acids from S-acylated proteins within the lyso-some (Lu et al., 1996). How the loss of this activity causes the death of central nervous system neurons is not known. 

The two subtypes of NCLs are due to deficiencies either in the palmitoyl protein thioesterase 1 (PPTl) protein or in the tripeptidyl peptidase 1 (TPPl) protein. The trial aforementioned by a cell therapy was comprised of neural stem/progenitor cells which constitutively synthesize and secrete both the PPTl and TPPl enzymes. In culture, these secreted enzymes are internalized by... 

Young E.P., Worthington V.C., Jackson M., Winchester B.G., Pre- and postnatal diagnosis of patients with CLNl and CLN2 by assay of palmitoyl-protein thioesterase and tripeptidyl-peptidase I activities, European Journal of Paediatric Neurology 5 Suppl A (2001) 193-196. 

Late infantile neuronal ceroid lipofuscinosis (CLN2) Tripeptidyl peptidase 1 llpl5.5 204500... 

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