3.4.14.11: Xaa-Pro dipeptidyl-peptidase
This is an abbreviated version!
For detailed information about Xaa-Pro dipeptidyl-peptidase, go to the full flat file.
Word Map on EC 3.4.14.11
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3.4.14.11
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lactis
-
subsp
-
food industry
-
cremoris
-
streptococcus
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milk
-
lactobacillus
-
lactococci
-
thermophilus
-
proline-specific
-
helveticus
-
venema
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3.4.14.5
-
pyroglutamyl
-
microbiol
-
x-prolyl-dipeptidyl
-
mutans
-
diprotin
-
cystyl
-
mayo
-
imino
-
endopeptidase
-
exopeptidases
-
reinke
-
whey
-
saxagliptin
-
casei
-
synthesis
- 3.4.14.11
- lactis
-
subsp
- food industry
- cremoris
- streptococcus
- milk
- lactobacillus
-
lactococci
- thermophilus
-
proline-specific
- helveticus
-
venema
-
3.4.14.5
-
pyroglutamyl
-
microbiol
-
x-prolyl-dipeptidyl
- mutans
- diprotin
-
cystyl
-
mayo
-
imino
- endopeptidase
-
exopeptidases
-
reinke
- whey
- saxagliptin
- casei
- synthesis
Reaction
Hydrolyses Xaa-Pro-/- bonds to release unblocked, N-terminal dipeptides from substrates including Ala-Pro-/-p-nitroanilide and (sequentially) Tyr-Pro-/-Phe-Pro-/-Gly-Pro-/-Ile =
Synonyms
DAP, LGAS_0712, More, Pep-XP, PepX, PepXP, prolyl dipeptidyl aminopeptidase, X-PDAP, X-Pro dipeptidyl-peptidase, X-prolyl dipeptidyl aminopeptidase, X-prolyl dipeptidyl peptidase, X-prolyl-dipeptidyl aminopeptidase
ECTree
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pH Stability
pH Stability on EC 3.4.14.11 - Xaa-Pro dipeptidyl-peptidase
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unstable below, the enzyme from Streptococcus thermophilus is more rapidly denatured than the enzyme from Lactobacillus lactis
647175
5
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unstable below, the enzyme from Streptococcus thermophilus is more rapidly denatured than the enzyme from Lactobacillus lactis
647175