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Literature summary extracted from

  • Du, P.; An, L.; Qiu, F.; Lu, G.
    Peptidase activities of tripeptidyl peptidase I (TPP I): exopeptidase and endopeptidase (2006), Chem. Res. Chin. Univ., 22, 65-67.
No PubMed abstract available

Organism

EC Number Organism UniProt Comment Textmining
3.4.14.9 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.14.9 kidney
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.14.9 Ala-Ala-Phe-7-amido-4-methylcoumarin + H2O
-
 Rattus norvegicus Ala-Ala-Phe + 7-amino-4-methylcoumarin
-
 ?
3.4.14.9 angiotensin II + H2O
-
 Rattus norvegicus ? + Asp-Arg-Val
-
 ?
3.4.14.9 Gly-Lys-Pro-Ile-Pro-Phe-Phe-Arg-Leu-Lys + H2O
-
 Rattus norvegicus Gly-Lys-Pro-Ile-Pro-Phe + Phe-Arg-Leu-Lys
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.14.9 TPP I
-
 Rattus norvegicus
3.4.14.9 tripeptidyl peptidase I shows tripeptidyl peptidase activity and pepstatin insensitive carboxyl endopeptidase activity Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.14.9 additional information
-
 the optimum pH of TPP 1 is dependent on the substrate used Rattus norvegicus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.4.14.9 3 6 at pH 3.0 the activity of TPP I is less than 75% of its maximal activity at pH 4.5, most stable at pH 3-4, no activity at pH above 6.0 Rattus norvegicus