| http://purl.uniprot.org/citations/10679303 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
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| http://purl.uniprot.org/citations/10679303 | http://www.w3.org/2000/01/rdf-schema#comment | "Endopeptidase activities of the CLN2 gene product (Cln2p)/tripeptidyl peptidase I (TPP-I), purified from rat spleen, were studied using the synthetic fluorogenic substrates. We designed and constructed decapeptides, based on the known sequence cleavage specificities of bacterial pepstatin-insensitive carboxyl proteases (BPICP). MOCAc-Gly-Lys-Pro-Ile-Pro-Phe-Phe-Arg-Leu-Lys(Dnp)r-NH(2) is readily hydrolyzed by Cln2p/TPP-I (K(cat)/K(m) = 7.8 s(-1) mM(-1)). The enzyme had a maximal activity at pH 3.0 for an endopeptidase substrate, but at pH 4.5 with respect to tripeptidyl peptidase activity. Both endopeptidase and tripeptidyl peptidase activities were strongly inhibited by Ala-Ala-Phe-CH(2)Cl, but not inhibited by tyrostatin, an inhibitor of bacterial pepstatin-insensitive carboxyl proteases, pepstatin, or inhibitors of serine proteases. Fibroblasts from classical late infantile neuronal ceroid lipofuscinosis patients have less than 5% of the normal tripeptidyl peptidase activity and pepstatin-insensitive endopeptidase activity. Cln2p/TPP-I is a unique enzyme with both tripeptidyl peptidase and endopeptidase activities for certain substrate specificity."xsd:string |
| http://purl.uniprot.org/citations/10679303 | http://purl.org/dc/terms/identifier | "doi:10.1006/bbrc.2000.2207"xsd:string |
| http://purl.uniprot.org/citations/10679303 | http://purl.uniprot.org/core/author | "Oda K."xsd:string |
| http://purl.uniprot.org/citations/10679303 | http://purl.uniprot.org/core/author | "Kominami E."xsd:string |
| http://purl.uniprot.org/citations/10679303 | http://purl.uniprot.org/core/author | "Ezaki J."xsd:string |
| http://purl.uniprot.org/citations/10679303 | http://purl.uniprot.org/core/author | "Takeda-Ezaki M."xsd:string |
| http://purl.uniprot.org/citations/10679303 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10679303 | http://purl.uniprot.org/core/name | "Biochem Biophys Res Commun"xsd:string |
| http://purl.uniprot.org/citations/10679303 | http://purl.uniprot.org/core/pages | "904-908"xsd:string |
| http://purl.uniprot.org/citations/10679303 | http://purl.uniprot.org/core/title | "Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2 protein which is deficient in classical late infantile neuronal ceroid lipofuscinosis."xsd:string |
| http://purl.uniprot.org/citations/10679303 | http://purl.uniprot.org/core/volume | "268"xsd:string |
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