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3.4.11.4: tripeptide aminopeptidase

This is an abbreviated version!
For detailed information about tripeptide aminopeptidase, go to the full flat file.

Word Map on EC 3.4.11.4

Reaction

release of the N-terminal residue from a tripeptide =

Synonyms

alanine-phenylalanine-proline arylamidase, alpha-aminoacyl-dipeptide hydrolase, aminoexotripeptidase, aminopeptidase, human liver, aminotripeptidase, arginyl tri-peptidase, ec 3.4.1.3, EC 3.4.14.10, imidoendopeptidase, lymphopeptidase, PepB, PepT, peptidase B, peptidase T, prolyl tripeptidyl aminopeptidase, PTP, PTP39, TPP I, TPP II, TPPII, tripeptidase, tripeptidyl aminopeptidase, tripeptidyl exopeptidase II, tripeptidyl peptidase II, tripeptidyl-peptidase I, tripeptidyl-peptidase II

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.4 tripeptide aminopeptidase

Engineering

Engineering on EC 3.4.11.4 - tripeptide aminopeptidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C25S
-
mutant enzyme shows no loss or decrease of enzymatic activity
DELTA1-119
-
inactive mutant enzyme
DELTA1-159
-
inactive mutant enzyme
DELTA1-208
-
inactive mutant enzyme
DELTA1-66
-
mutant enzyme requires a concentration of Zn2+ ion at least ten-fold higher to reach maximal activity without significantly affecting kinetic parameters such as Km and Vmax compared to the full length tripeptidase
DELTA211-410
-
inactive mutant enzyme
DELTA271-410
-
inactive mutant enzyme
DELTA291-410
-
inactive mutant enzyme
DELTA361-410
-
inactive mutant enzyme
D276A
-
kcat/KM is 21% of wild-type value
D327A
-
kcat/KM is 6% of wild-type value
D360A
-
kcat/KM is 3% of wild-type value
E272A
-
kcat/KM is 3% of wild-type value
S475L
-
kcat/KM is 0.4% of wild-type value
E205A
-
inactive
E205Q
-
inactive
E636A
-
reduced activity
S603A
-
inactive