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Information on EC 3.4.14.11 - Xaa-Pro dipeptidyl-peptidase
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EC Tree
3.4.14.11 Xaa-Pro dipeptidyl-peptidaseSpecify your search results
Word Map
- 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
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pepxp, x-prolyl dipeptidyl peptidase, prolyl dipeptidyl aminopeptidase, xaa-pro dipeptidyl-peptidase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PepX
PepXP
prolyl dipeptidyl aminopeptidase
X-PDAP
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-
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X-Pro dipeptidyl-peptidase
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-
-
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X-prolyl dipeptidyl aminopeptidase
X-prolyl dipeptidyl peptidase
X-prolyl-dipeptidyl aminopeptidase
additional information
PepX
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X-prolyl dipeptidyl aminopeptidase
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X-prolyl dipeptidyl peptidase
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X-prolyl-dipeptidyl aminopeptidase
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X-prolyl-dipeptidyl aminopeptidase
Lacticaseibacillus casei Lc 279
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
a member of peptidase family S15. The reaction is similar to that catalyzed by dipeptidyl-peptidase IV of animals
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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-
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-
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CAS REGISTRY NUMBER
COMMENTARY
54249-88-6
not distinguishable from EC 3.4.14.5 in Chemical Abstracts
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-casein + H2O
?
-
function of the enzyme is to cleave the proline-rich sequence of beta-casein
-
-
?
Glu-Pro-7-amido-4-methylcoumarin + H2O
Glu-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Ala-7-amido-4-methylcoumarin + H2O
Gly-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-Arg-Pro + H2O
Gly-Pro + Arg-Pro
-
as active as Gly-Pro-4-nitroanilide
-
-
?
Ile-Pro-Ile + H2O
Ile-Pro + Ile
-
34% of the activity with Gly-Pro-4-nitroanilide
-
-
?
L-Ala-L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala-L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
Leu-Pro-7-amido-4-methylcoumarin + H2O
Leu-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Lys-Ala-Val-Pro-Tyr-Pro-Gln + H2O
?
-
fragment 176-182 of beta-casein
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-
?
Lys-Pro-7-amido-4-methylcoumarin + H2O
Lys-Pro + 7-amino-4-methylcoumarin
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-
-
-
?
Lys-Pro-p-nitroanilide + H2O
Lys-Pro + p-nitroaniline
-
85% of the activity with Arg-Pro-p-nitroanilide
-
-
?
Phe-Pro-7-amido-4-methylcoumarin + H2O
Phe-Pro + 7-amino-4-methylcoumarin
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-
-
-
?
Tyr-Pro-Phe-Pro-Gly-Pro-Ile + H2O
Tyr-Pro + Phe-Pro-Gly-Pro-Ile
-
i.e. BCM-7, beta-casomorphin 7
-
-
?
Val-Pro-Leu + H2O
Val-Pro + Leu
-
83% of the activity with Gly-Pro-nitroanilide
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-
?
Ala-Ala 4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
-
2% of the activity with Gly-Pro 4-nitroanilide
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-
?
Ala-Pro-4-nitroanilide + H2O
Ala-Pro + 4-nitroaniline
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-
-
?
Ala-Pro-4-nitroanilide + H2O
Ala-Pro + 4-nitroaniline
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-
-
?
Ala-Pro-Gly + H2O
Ala-Pro + Gly
-
11% of the activity with Gly-Pro 4-nitroanilide
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-
?
Ala-Pro-Gly + H2O
Ala-Pro + Gly
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72% of the activity with Gly-Pro-4-nitroanilide
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-
?
Arg-Pro 4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
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best substrate
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-
?
Arg-Pro 4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
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130% of the activity with Gly-Pro 4-nitroanilide
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-
?
Arg-Pro 4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
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-
-
-
?
Arg-Pro 4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
-
60.5% of the activity with Gly-Pro-7-amido-4-methylcoumarin
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-
?
Arg-Pro 4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
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55% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Arg-Pro-4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
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-
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-
?
beta-casomorphin + H2O
?
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the hydrolysis of the tripeptide Gly-Pro-Ile is slower, after the release of the dipeptide Tyr-Pro, the resulting pentapeptide does not accumulate in the medium, rather the dipeptide Phe-Pro is released very rapidly
?
beta-casomorphin + H2O
?
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-
main split products: Tyr-Pro and Phe-Pro
?
beta-casomorphin + H2O
?
-
Tyr-Pro-Phe-Pro-Gly-Pro-Ile
the hydrolysis of the tripeptide Gly-Pro-Ile is slower, after the release of the dipeptide Tyr-Pro, the resulting pentapeptide does not accumulate in the medium, rather the dipeptide Phe-Pro is released very rapidly
?
beta-casomorphin + H2O
?
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fragment 60-66 of beta-casein or beta-casomorphin
main split products: Tyr-Pro, Phe-Pro and Gly-Pro-Ile
?
beta-casomorphin + H2O
?
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Tyr-Pro-Phe-Pro-Gly-Pro-Ile
the hydrolysis of the tripeptide Gly-Pro-Ile is slower
?
beta-casomorphin + H2O
?
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main split products: Tyr-Pro and Phe-Pro
?
beta-casomorphin + H2O
?
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main split products: Tyr-Pro and Phe-Pro
?
Gly-L-Pro 4-nitroanilide + H2O
Gly-L-Pro + 4-nitroaniline
6% of the activity with L-Ala-L-Pro-4-nitroanilide
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-
?
Gly-L-Pro 4-nitroanilide + H2O
Gly-L-Pro + 4-nitroaniline
6% of the activity with L-Ala-L-Pro-4-nitroanilide
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-
?
Gly-L-Pro 4-nitroanilide + H2O
Gly-L-Pro + 4-nitroaniline
-
16% of the activity with L-Ala-L-Pro 4-nitroanilide
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-
?
Gly-Pro 4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
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-
-
-
?
Gly-Pro 4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
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-
-
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?
Gly-Pro 4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
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-
-
-
?
Gly-Pro 4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
25.5% of the activity with Gly-Pro-7-amido-4-methylcoumarin
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?
Gly-Pro-4-nitroanilide + H2O
Gly + Pro-4-nitroanilide
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?
Gly-Pro-4-nitroanilide + H2O
Gly + Pro-4-nitroanilide
Lactococcus lactis ssp. lactis NRRL B-1821
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?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
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?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
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?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
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?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
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?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
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?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
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?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
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?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
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?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
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?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
Lacticaseibacillus casei Lc 279
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?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
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?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
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?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
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-
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?
L-Ala-L-Pro 4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
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-
?
L-Ala-L-Pro 4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
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-
-
?
L-Ala-L-Pro 4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
-
-
-
?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
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-
-
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?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
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-
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?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
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-
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?
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
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best substrate
-
-
?
L-Ala-L-Pro-L-Arg + H2O
L-Ala-L-Pro + L-Arg
-
-
-
?
L-Ala-L-Pro-L-Ser + H2O
L-Ala-L-Pro + L-Ser
-
-
-
?
L-Ala-L-Pro-L-Tyr + H2O
L-Ala-L-Pro + L-Tyr
-
-
-
?
L-Arg-L-Pro 4-nitroanilide + H2O
L-Arg-L-Pro + 4-nitroaniline
59% of the activity with L-Ala-L-Pro-4-nitroanilide
-
-
?
L-Arg-L-Pro 4-nitroanilide + H2O
L-Arg-L-Pro + 4-nitroaniline
59% of the activity with L-Ala-L-Pro-4-nitroanilide
-
-
?
L-Arg-L-Pro 4-nitroanilide + H2O
L-Arg-L-Pro + 4-nitroaniline
-
13.6% of the activity with L-Ala-L-Pro 4-nitroanilide
-
-
?
Lys-Ala-7-amido-4-methylcoumarin + H2O
Lys-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
Lys-Ala-7-amido-4-methylcoumarin + H2O
Lys-Ala + 7-amino-4-methylcoumarin
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9.9% of the activity with Gly-Pro-7-amido-4-methylcoumarin
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-
?
VYPFPGPIPN + H2O
?
substrate opioid precursor peptide, which is released during casein hydrolysis
-
-
?
VYPFPGPIPN + H2O
?
substrate opioid precursor peptide, which is released during casein hydrolysis
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?
additional information
?
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the enzyme is likely a serine proteinase
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?
additional information
?
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the enzyme is likely a serine proteinase
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?
additional information
?
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Lactobacillus gasseri me-284
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the enzyme is likely a serine proteinase
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?
additional information
?
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no substrate inhibition is determined
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?
additional information
?
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no substrate inhibition is determined
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?
additional information
?
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-
no activity with Ala-Leu-Ala
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?
additional information
?
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no activity with bradikinins with N-terminal sequences Arg-Pro-Pro- and Lys-Pro-Pro-
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?
additional information
?
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no activity with Pro-p-nitroanilide or azocasein
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?
additional information
?
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maximal activity with Pro in the N-penultimate position
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
beta-casein + H2O
?
-
function of the enzyme is to cleave the proline-rich sequence of beta-casein
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
chloroform
reduced the enzyme activity during purification
KCl
up to 300 mM, slight activitation. Inhibitory above 500 mM
Na+
up to 300 mM, slight activitation. Inhibitory above 500 mM
Phenylmethanesulphonyl fluoride
-
0.1 mM, 20 min at 40°C, 40% loss of activity. 1 mM, complete inhibition after 20 min
Triton X-100
reduces the enzyme activity during purification
diisopropylfluorophosphate