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Literature summary for 3.4.14.9 extracted from

  • Lin, L.; Sohar, I.; Lackland, H.; Lobel, P.
    The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH (2001), J. Biol. Chem., 276, 2249-2255.
    View publication on PubMed
Search for more literature for 3.4.14.9

Cloned(Commentary)

Cloned (Comment) Organism
C-terminal hexahistidine-tagged human CLN2p/tripeptidyl-peptidase I produced from insect cells transfected with a baculovirus vector Homo sapiens

Protein Variants

Protein Variants Comment Organism
D360A lack of enzyme activity and processing Homo sapiens
D517A lack of enzyme activity and processing Homo sapiens
S475 inactive mutant enzyme Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline
-
 Homo sapiens
3,4-dichloroisocoumarin
-
 Homo sapiens
Ala-Ala-Phe-CH2Cl
-
 Homo sapiens
diisopropylfluorophosphate
-
 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
lysosome
-
 Homo sapiens 5764
-

Organism

Organism UniProt Comment Textmining
Homo sapiens O14773
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the protein is synthesized as an inactive zymogen that is autocatalytically converted to an active serine protease at acidic pH, removal of a 19-residue signal peptide Homo sapiens

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5 5 hydrolysis of Ala-Ala-Phe-7-amido-4-methylcoumarin Homo sapiens

pH Range

pH Minimum pH Maximum Comment Organism
4 5.5 about 55% of maximal activity at pH 4.0 and at pH 5.5, hydrolysis of Ala-Ala-Phe-7-amido-4-methylcoumarin Homo sapiens