Information on EC 3.4.14.11 - Xaa-Pro dipeptidyl-peptidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.4.14.11
-
RECOMMENDED NAME
GeneOntology No.
Xaa-Pro dipeptidyl-peptidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
a member of peptidase family S15. The reaction is similar to that catalyzed by dipeptidyl-peptidase IV of animals
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
54249-88-6
not distinguishable from EC 3.4.14.5 in Chemical Abstracts
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
strain Bl 536
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-
Manually annotated by BRENDA team
strain Bl 536
-
-
Manually annotated by BRENDA team
strain L10
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-
Manually annotated by BRENDA team
strain La 4962
-
-
Manually annotated by BRENDA team
strain L26
-
-
Manually annotated by BRENDA team
bulgaricus LBU-147
-
-
Manually annotated by BRENDA team
strain 53/7
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-
Manually annotated by BRENDA team
strain CB1
-
-
Manually annotated by BRENDA team
nTR
-
-
Manually annotated by BRENDA team
P8-2-47
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Ala-Ala 4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
show the reaction diagram
Ala-Pro-4-nitroanilide + H2O
Ala-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Ala-Pro-Gly + H2O
Ala-Pro + Gly
show the reaction diagram
Arg-Pro 4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
show the reaction diagram
Arg-Pro-4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
show the reaction diagram
Arg-Pro-p-nitroanilide + H2O
Arg-Pro + p-nitroaniline
show the reaction diagram
-
-
-
-
?
beta-casein + H2O
?
show the reaction diagram
-
function of the enzyme is to cleave the proline-rich sequence of beta-casein
-
-
-
beta-casomorphin + H2O
?
show the reaction diagram
Glu-Pro-7-amido-4-methylcoumarin + H2O
Glu-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Gly-Ala-7-amido-4-methylcoumarin + H2O
Gly-Ala + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Gly-L-Pro 4-nitroanilide + H2O
Gly-L-Pro + 4-nitroaniline
show the reaction diagram
Gly-Pro 4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
show the reaction diagram
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
Gly-Pro-Ala + H2O
Gly-Pro + Ala
show the reaction diagram
Gly-Pro-Arg-Pro + H2O
Gly-Pro + Arg-Pro
show the reaction diagram
-
as active as Gly-Pro-4-nitroanilide
-
-
?
Gly-Pro-Gly-Gly + H2O
Gly-Pro + Gly-Gly
show the reaction diagram
-
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
show the reaction diagram
His-Pro-Leu + H2O
His-Pro + Leu
show the reaction diagram
-
-
-
-
?
His-Pro-Tyr + H2O
His-Pro + Tyr
show the reaction diagram
-
-
-
-
?
Ile-Pro-Ile + H2O
Ile-Pro + Ile
show the reaction diagram
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34% of the activity with Gly-Pro-4-nitroanilide
-
-
?
L-Ala-L-Pro 4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
show the reaction diagram
L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala-L-Pro + 4-nitroaniline
show the reaction diagram
L-Ala-L-Pro-L-Arg + H2O
L-Ala-L-Pro + L-Arg
show the reaction diagram
L-Ala-L-Pro-L-Ser + H2O
L-Ala-L-Pro + L-Ser
show the reaction diagram
L-Ala-L-Pro-L-Tyr + H2O
L-Ala-L-Pro + L-Tyr
show the reaction diagram
L-Arg-L-Pro 4-nitroanilide + H2O
L-Arg-L-Pro + 4-nitroaniline
show the reaction diagram
L-Arg-L-Pro-L-Ala + H2O
L-Arg-L-Pro + L-Ala
show the reaction diagram
-
-
-
?
L-Asp-L-Pro-L-Ala + H2O
L-Asp-L-Pro + L-Ala
show the reaction diagram
-
-
-
?
L-Ser-L-Pro-L-Ala + H2O
L-Ser-L-Pro + L-Ala
show the reaction diagram
-
-
-
?
L-Tyr-L-Pro-L-Ala + H2O
L-Tyr-L-Pro + L-Ala
show the reaction diagram
-
-
-
?
Leu-Ala-Pro + H2O
?
show the reaction diagram
-
-
-
-
?
Leu-Pro-7-amido-4-methylcoumarin + H2O
Leu-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Lys-Ala-7-amido-4-methylcoumarin + H2O
Lys-Ala + 7-amino-4-methylcoumarin
show the reaction diagram
Lys-Ala-Val-Pro-Tyr-Pro-Gln + H2O
?
show the reaction diagram
-
fragment 176-182 of beta-casein
-
-
?
Lys-Pro-7-amido-4-methylcoumarin + H2O
Lys-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Lys-Pro-p-nitroanilide + H2O
Lys-Pro + p-nitroaniline
show the reaction diagram
-
85% of the activity with Arg-Pro-p-nitroanilide
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-
?
Phe-Pro-7-amido-4-methylcoumarin + H2O
Phe-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Tyr-Pro-Phe + H2O
Tyr-Pro + Phe
show the reaction diagram
-
-
-
-
?
Val-Pro-Leu + H2O
Val-Pro + Leu
show the reaction diagram
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83% of the activity with Gly-Pro-nitroanilide
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-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-casein + H2O
?
show the reaction diagram
-
function of the enzyme is to cleave the proline-rich sequence of beta-casein
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
0.1-2.5 mM, 40C, 15 min, activation
Fe2+
-
weak activation
K+
-
10-50 mM, 40C, 15 min, activation
Na+
-
10-50 mM, 40C, 15 min, activation
Zn2+
-
weak activation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
3,4-dichloroisocoumarin
Ca2+
-
1 mM, 89% residual activity
diisopropylfluorophosphate
Diprotin A
-
IC50: 0.26 mM
Diprotin B
-
IC50: 0.6 mM
iodoacetate
KCl
-
up to 300 mM, slight activitation. Inhibitory above 500 mM
L-Phe-L-Pro
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10 mM, 38% inhibition, mixed-ype inhibition
L-Tyr-L-Pro
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10 mM, 28% inhibition, mixed-type inhibition
Na+
-
up to 300 mM, slight activitation. Inhibitory above 500 mM
p-chloromercuribenzoate
-
competitive
p-hydroxymercuribenzoate
-
reactivated by DTT
pefabloc
-
1 mM, 35% residual activity
Phenylmethanesulphonyl fluoride
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0.1 mM, 20 min at 40C, 40% loss of activity. 1 mM, complete inhibition after 20 min
phenylmethylsulfonyl fluoride
PMSF
-
1 mM, 8.4% residual activity
Urea
-
2.0 M
Val-pyrrolidide
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IC50: 0.03 mM
additional information
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not: DTT, 1.0-19 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
cysteine
-
weak activation
dithiothreitol
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weak activation
glycerol
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up to 25%, enhances activity
KCl
-
up to 300 mM, slight activitation. Inhibitory above 500 mM
Na+
-
up to 300 mM, slight activitation. Inhibitory above 500 mM
Triglyme
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up to 25%, enhances activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
Ala-Pro-4-nitroanilide
-
pH 7.5, 37C
0.92
Arg-Pro-p-nitroanilide
-
-
0.0457
Glu-Pro-7-amido-4-methylcoumarin
-
-
0.385
Gly-Ala 4-methylcoumarin 7-amide
-
-
0.11
Gly-L-Pro 4-nitroanilide
-
pH 6.5, 37C
0.107 - 0.55
Gly-Pro 4-nitroanilide
0.192 - 3.1
Gly-Pro-4-nitroanilide
0.0141 - 0.2
Gly-Pro-7-amido-4-methylcoumarin
1.3 - 1.53
L-Ala-L-Pro 4-nitroanilide
0.14
L-Ala-L-Pro-L-Arg
-
pH 6.5, 37C
0.53
L-Ala-L-Pro-L-Ser
-
pH 6.5, 37C
0.17
L-Ala-L-Pro-L-Tyr
-
pH 6.5, 37C
1.5
L-Arg-L-Pro 4-nitroanilide
-
pH 6.5, 37C
0.24
L-Arg-L-Pro-L-Ala
-
pH 6.5, 37C
1.23
L-Asp-L-Pro-L-Ala
-
pH 6.5, 37C
0.54
L-Ser-L-Pro-L-Ala
-
pH 6.5, 37C
0.12
L-Tyr-L-Pro-L-Ala
-
pH 6.5, 37C
0.0092
Leu-Pro-7-amido-4-methylcoumarin
-
-
0.088 - 0.231
Lys-Ala-7-amido-4-methylcoumarin
0.0146
Lys-Pro-7-amido-4-methylcoumarin
-
-
0.0124
Phe-Pro-7-amido-4-methylcoumarin
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
26
Ala-Ala-7-amido-4-methylcoumarin
Lactococcus lactis
-
-
181
Arg-Pro 4-nitroanilide
Lactococcus lactis
-
-
62.9
Glu-Pro-7-amido-4-methylcoumarin
Lactococcus lactis
-
-
2.1
Gly-Ala-7-amido-4-methylcoumarin
Lactococcus lactis
-
-
178
Gly-Pro 4-nitroanilide
Lactococcus lactis
-
-
62.1 - 69.8
Gly-Pro-7-amido-4-methylcoumarin
2180
Gly-Pro-Ala
Lactococcus lactis
-
-
46.4
Gly-Pro-Gly-Gly
Lactococcus lactis
-
-
418
His-Pro-Leu
Lactococcus lactis
-
-
670
His-Pro-Tyr
Lactococcus lactis
-
-
57.2
L-Ala-L-Pro-L-Arg
Lactobacillus helveticus
-
pH 6.5, 37C
95.9
L-Ala-L-Pro-L-Ser
Lactobacillus helveticus
-
pH 6.5, 37C
43.5
L-Ala-L-Pro-L-Tyr
Lactobacillus helveticus
-
pH 6.5, 37C
133
L-Arg-L-Pro-L-Ala
Lactobacillus helveticus
-
pH 6.5, 37C
199
L-Asp-L-Pro-L-Ala
Lactobacillus helveticus
-
pH 6.5, 37C
233
L-Ser-L-Pro-L-Ala
Lactobacillus helveticus
-
pH 6.5, 37C
145
L-Tyr-L-Pro-L-Ala
Lactobacillus helveticus
-
pH 6.5, 37C
120
Leu-Ala-Pro
Lactococcus lactis
-
-
43.4
Leu-Pro-7-amido-4-methylcoumarin
Lactococcus lactis
-
-
17.1
Lys-Ala-7-amido-4-methylcoumarin
Lactococcus lactis
-
-
61.6
Lys-Pro-7-amido-4-methylcoumarin
Lactococcus lactis
-
-
78.4
Phe-Pro-7-amido-4-methylcoumarin
Lactococcus lactis
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
409
L-Ala-L-Pro-L-Arg
Lactobacillus helveticus
-
pH 6.5, 37C
202272
181
L-Ala-L-Pro-L-Ser
Lactobacillus helveticus
-
pH 6.5, 37C
202270
256
L-Ala-L-Pro-L-Tyr
Lactobacillus helveticus
-
pH 6.5, 37C
202275
552
L-Arg-L-Pro-L-Ala
Lactobacillus helveticus
-
pH 6.5, 37C
202273
162
L-Asp-L-Pro-L-Ala
Lactobacillus helveticus
-
pH 6.5, 37C
202274
431
L-Ser-L-Pro-L-Ala
Lactobacillus helveticus
-
pH 6.5, 37C
202271
1210
L-Tyr-L-Pro-L-Ala
Lactobacillus helveticus
-
pH 6.5, 37C
202276
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.26
Diprotin A
Lactococcus lactis
-
IC50: 0.26 mM
0.6
Diprotin B
Lactococcus lactis
-
IC50: 0.6 mM
0.03
Val-pyrrolidide
Lactococcus lactis
-
IC50: 0.03 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22.2
-
pH 6.5, 37C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
little variation in activity in this range
6.5 - 8.2
-
hydrolysis of Gly-Pro-7-amido-4-methylcoumarin
7 - 7.5
-
hydrolysis of Gly-Pro 4-nitroanilide
7.2
-
assay at
9.5
-
and a second pH-optimum at pH 7.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
pH 5: about 50% of maximal activity, pH 9: about 60% of maximal activity
5 - 7
-
pH 5.0: 88% of maximal activity, pH 7.0: maximal activity
5.5 - 8
-
pH 5.5: about 50% of maximal activity, pH 8: about 65% of maximal activity
5.5 - 8.5
-
pH 5.5: 50% of maximal activity, pH 8.5: activity maximum
6 - 9
-
pH 6.0: about 90% of maximal activity, pH 9.0: about 85% of maximal activity, hydrolysis of Gly-Pro-4-nitroanilide
7
-
87% of maximum activity, Na2HPO4/KH2PO4 buffer
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 50
-
about 55% of activity maximum at 10C and 50C
10 - 65
-
10C: about 55% of activity maximum, 65C: 34% of activity maximum
20 - 55
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20C: about 30% of activity maximum, 55C: about 40% of activity maximum
20 - 65
-
about 30% of maximal activity at 20C and at 65C, hydrolysis of Gly-Pro-7-amido-4-methylcoumarin
30 - 50
-
50% of maximal activity at 30C, maximum at 40-50C
35 - 60
-
35C: about 50% of maximal activity, 60C: about 30% of maximal activity, hydrolysis of Gly-Pro-7-amido-4-methylcoumarin
40 - 50
-
40C: 95% of maximal activity, 50C: 98% of maximal activity
40 - 60
-
40C: about 15% of maximal activity, 60C: about 40% of maximal activity
65
-
8% residual activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
72000
-
x * 72000, native PAGE and SDS-PAGE
79000
-
x * 79000, native PAGE and SDS-PAGE
80000
-
2 * 80000, SDS-PAGE
82000
-
x * 82000, SDS-PAGE
85000
-
2 * 85000, SDS-PAGE with or without 2-mercaptoethanol
87000
-
1 * 87000, SDS-PAGE
88000
-
2 * 88000, SDS-PAGE
88450
-
calculation from nucleotide sequence analysis
90573
-
2 * 90573, calculation from nucleotide sequence
93000
-
gel filtration
125000
-
x * 125000, SDS-PAGE of recombinant protein
145000
-
2 * 145000, SDS-PAGE
150000
-
gel filtration
160000 - 180000
-
gel filtration
160000
-
gel filtration
165000
-
gel filtration
170000
-
gel filtration
190000
-
gel filtration
270000
-
gel filtration
280000
-
gel filtration
additional information
-
identification of the active site serine
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
trimer
additional information
-
each monomer is composed of four domains. The larger one presents an alpha/beta hydrolase fold and comprises the active site serine. The specificity pocket is mainly built by residues from a small helical domain which is, together with the N-terminal domain, essential for dimerization
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop method
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 9
-
10 min, stable
647168
5.5 - 9
-
12 h, stable
36250
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
1 h, 20% loss of activity
5 - 40
-
stable for 60 min
50
-
15 days, 34% residual activity
60
-
1 min in absence of substrate, 96% loss of activity
70
-
1 min, complete loss of activity
additional information
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acetone
acetonitrile
-
allows a limited stability at 4C and no stability at 30C
dioxane
-
allows a limited stability at 4C and no stability at 30C
DMSO
-
up to 25% increase stability at 4C and at 30C
Ethanol
Glycerol
-
up to 25% increase stability at 4C and at 30C
N,N-dimethylformamide
-
increases stability at 4C and allow a limited stability at 30C
triglyme
-
up to 25% increase stability at 4C and at 30C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 60% glycerol, stable for 30 days
-
4C, 20 mM Tris buffer, 20% loss of activity after 1 h
-
4C, pH 8.0, stable
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Esherichia coli
-
expression in Pichia pastoris
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
low PepXP activity is a predictor for subspecies Lactococcus lactis lactis
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
food industry
Show AA Sequence (1838 entries)
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