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Literature summary 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

Cloned(Commentary)

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

Protein Variants

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.14.9 1,10-phenanthroline
-
 Homo sapiens
3.4.14.9 3,4-dichloroisocoumarin
-
 Homo sapiens
3.4.14.9 Ala-Ala-Phe-CH2Cl
-
 Homo sapiens
3.4.14.9 diisopropylfluorophosphate
-
 Homo sapiens

Localization

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

Organism

EC Number Organism UniProt Comment Textmining
3.4.14.9 Homo sapiens O14773
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.14.9 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)

EC Number Purification (Comment) Organism
3.4.14.9
-
 Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.14.9 4.5 5 hydrolysis of Ala-Ala-Phe-7-amido-4-methylcoumarin Homo sapiens

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.14.9 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