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3.4.14.9: tripeptidyl-peptidase I

This is an abbreviated version!
For detailed information about tripeptidyl-peptidase I, go to the full flat file.

Word Map on EC 3.4.14.9

Reaction

Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity =

Synonyms

aminopeptidase, tripeptidyl, I, AO090166000084, ceroid lipofuscinosis 2 protease, CLN2, CLN2 protein, CLN2p, EC 3.4.14.8, LPIC, lysosomal pepstatin insensitive protease, N-terminal tripeptidyl exopeptidase, SedB, SedC, SedD, sedolisin B, sedolisin C, sedolisin D, TPP I, TPP-I, Tpp1, TPP1F, TPPI, tripeptidyl aminopeptidase, tripeptidyl aminopeptidase I, tripeptidyl exopeptidase, tripeptidyl peptidase, tripeptidyl peptidase 1, tripeptidyl peptidase I, tripeptidyl peptidase-I, tripeptidyl-peptidase 1, tripeptidyl-peptidase I, TTP-I, v4-7

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.14 Dipeptidyl-peptidases and tripeptidyl-peptidases
                3.4.14.9 tripeptidyl-peptidase I

pH Optimum

pH Optimum on EC 3.4.14.9 - tripeptidyl-peptidase I

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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
endopeptidase
3.5
assay at
3.5 - 4
with substrate RWFVIQ-EDDnp
3.5 - 4.5
-
-
4.3
-
hydrolysis of Gly-Pro-Met 4-nitroanilide
4.5 - 5
hydrolysis of Ala-Ala-Phe-7-amido-4-methylcoumarin
5 - 5.5
-
hydrolysis of Gly-Pro-Met 2-naphthylamide or Ala-Ala-Phe 4-methylcoumarin 7-amide
5.5
with substrate and KWFFIQ-EDDnp
5.9
-
and a second optimum at pH 4.5, at pH 5.9 70% of the activity at pH 4.5
additional information
-
the optimum pH of TPP 1 is dependent on the substrate used