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Literature summary for 3.4.14.9 extracted from

  • Golabek, A.A.; Kida, E.; Walus, M.; Wujek, P.; Mehta, P.; Wisniewski, K.E.
    Biosynthesis, glycosylation, and enzymatic processing in vivo of human tripeptidyl-peptidase I (2003), J. Biol. Chem., 278, 7135-7145.
    View publication on PubMed
Search for more literature for 3.4.14.9

Cloned(Commentary)

Cloned (Comment) Organism
expression in Chinese hamster ovary cells under the control of the cytomegalovirus promoter Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
lysosome the conversion of the proenzyme into the mature form takes place in lysosomal compartment Homo sapiens 5764
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein all five potential N-glycosylation sites in the enzyme are utilized, some of its N-linked oligosaccharides are of the complex/hybrid type Homo sapiens
proteolytic modification the 68000 Da precursor polypeptide is converted to the mature enzyme of 48000 Da. Although tripeptidyl-peptidase I zymogen is capable of autoactivation in vitro, a serine protease that is sensitive to 4-(2-aminoethyl)-benzene-sulfonamide participates in processing of the proenzyme to the mature, active form in vivo Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
-
 Homo sapiens Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
 ?
additional information the enzyme removes tripeptides from the free N-termini of small polypeptides and also shows a minor endoprotease activity Homo sapiens ?
-
 ?