3.4.14.10: tripeptidyl-peptidase II
This is an abbreviated version!
For detailed information about tripeptidyl-peptidase II, go to the full flat file.
Word Map on EC 3.4.14.10
-
3.4.14.10
-
exopeptidase
-
tppii
-
ceroid
-
butabindide
-
subtilisin-like
-
oligopeptidase
-
collagen-related
-
cholecystokinin-8
-
gly-pro-x
-
medicine
- 3.4.14.10
-
exopeptidase
- tppii
-
ceroid
- butabindide
-
subtilisin-like
-
oligopeptidase
-
collagen-related
- cholecystokinin-8
-
gly-pro-x
- medicine
Reaction
Release of an N-terminal tripeptide from a polypeptide =
Synonyms
aminopeptidase, tripeptidyl, II, cholecystokinin-inactivating peptidase, dTPP II, EC 3.4.14.8, hTPP II, mTPP II, PTP-A, TPII, TPP, TPP II, TPP-2, TPP-II, TPP2, TPPII, tripeptidyl aminopeptidase, tripeptidyl aminopeptidase I, tripeptidyl aminopeptidase I I, tripeptidyl aminopeptidase II, tripeptidyl peptidase, tripeptidyl peptidase II, tripeptidyl-peptidase-II, tripeptidylpeptidase II, TY-21 TPP
ECTree
3.4.14.10 tripeptidyl-peptidase IIAdvanced search results
results (
results (Engineering
Engineering on EC 3.4.14.10 - tripeptidyl-peptidase II
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D387G
D44A
-
catalytic activity of the mutant enzyme is at least one order of magnitude lower than that of the wild-type enzyme
H264A
-
catalytic activity of the mutant enzyme is at least one order of magnitude lower than that of the wild-type enzyme
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
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
D387G
mutant shows bell-shaped pH-dependence of kcat, possibly due to an impaired protonation of the leaving group
E331K
the catalytic efficiency is reduced 20000fold for the E331K variant compared to the wild type enzyme
E331Q
G375D
H267A
additional information
D387G
the pKa values of mutant D387G for kcat (app) increase when Asp-387 is changed to glycine. Mutant shows a bell-shaped pH-dependence of kcat(app), possibly due to an impaired protonation of the leaving group. Mutant shows a decresed kcat for all substrates and a highly decreased kcat/Km compared to wild-type. In contrast to wild-type at higher pH the kcat (app) value decreases
E331Q
the catalytic efficiency is reduced 400fold for the E331Q variant compared to the wild type enzyme
E331Q
mutant has a 2-3 orders of magnitude decreased kcat app/KM compared to wild-type, mostly dependent on an increase in KM
G375D
mutant has only 0.1% activity of wild-type at pH 7.5. Mutant shows a marked decrease in pH optimum compared to wild-type
H267A
mutant shows bell-shaped pH-dependence of kcat, possibly due to an impaired protonation of the leaving group
H267A
mutant shows mostly a decresed kcat for all substrates and a highly decreased kcat/Km between 2 to fold orders of magnitude compared to wild-type. kcat shows a higher rise with pH in mutant H267A than in wild-type with substrate Ala-Ala-Phe-4-nitroanilide but at pH more than 7.6 kcat (app) decreases for substrate Ala-Ala-Phe-4-nitroanilide, resulting in a significantly better fit for a bell-shaped curve than for a sigmoidal
additional information
-
the recombinant human TPP II and murine TPP II display different association/dissociation characteristics when overexpressed in human 293-cells. The human enzyme is mainly in a nonassociated, inactive state, whereas the murine enzyme forms active oligomers. The formation of the active complex is profoundly influenced by a single amino acid difference: Gly252 in mouse and Arg252 in human
additional information
-
enzyme from an alternatively spliced cDNA variant contains an additional 39 bp, encoding 13 amino acids in the C-terminal end of the protein forms a larger complex. The C-terminal 13 amino acids are important for aggregation of subunits
additional information
-
the recombinant human TPP II and murine TPP II display different association/dissociation characteristics when overexpressed in human 293-cells. The human enzyme is mainly in a nonassociated, inactive state, whereas the murine enzyme forms active oligomers. The formation of the active complex is profoundly influenced by a single amino acid difference: Gly252 in mouse and Arg252 in human
