Literature summary for 3.4.14.10 extracted from

Hilbi, H.; Jozsa, E.; Tomkinson, B.
Identification of the catalytic triad in tripeptidyl-peptidase II through site-directed mutagenesis (2002), Biochim. Biophys. Acta, 1601, 149-154.

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Protein Variants

Protein Variants	Comment	Organism
D44A	catalytic activity of the mutant enzyme is at least one order of magnitude lower than that of the wild-type enzyme	Homo sapiens
H264A	catalytic activity of the mutant enzyme is at least one order of magnitude lower than that of the wild-type enzyme	Homo sapiens
N362A	catalytic activity of the mutant enzyme is at least one order of magnitude lower than that of the wild-type enzyme, mutation effects the quarternary structure of the endogenously expressed TPP II, resulting in formation of an active, larger complex of more than 10000 Da	Homo sapiens
S449A	inactive mutant enzyme, mutation effects the quarternary structure of the endogenously expressed TPP II, resulting in formation of an active, larger complex of more than 10000 Da	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Ala-Ala-Phe-p-nitroanilide + H2O	-	Homo sapiens	Ala-Ala-Phe + p-nitroaniline	-	?

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Release 2023.1 (January 2023)