Information on EC 3.4.13.9 - Xaa-Pro dipeptidase

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

EC NUMBER
COMMENTARY hide
3.4.13.9
-
RECOMMENDED NAME
GeneOntology No.
Xaa-Pro dipeptidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
hydrolysis of Xaa-/-Pro dipeptides; also acts on aminoacyl-hydroxyamine analogues. No action on Pro-Pro
show the reaction diagram
hydrolysis of Xaa-/-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-Pro
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
dipeptide hydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-32-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain JD6.5
-
-
Manually annotated by BRENDA team
strain JD6.5
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
random source, mixed breed dogs, gene pepQ
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Lactococcus lactis NRRL B-1821
gene pepQ; strain NRRL B-1821, gene pepQ
SwissProt
Manually annotated by BRENDA team
monkey
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Oenococcus oeni is the principal microorganism responsible for the malolactic fermentation, which decreases total acidity and improves the quality and stability of wine, strain IOEB 8413, gene pepQ
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl soman + H2O
?
show the reaction diagram
-
-
-
-
?
Ala-Ala + H2O
Ala + Ala
show the reaction diagram
-
-
-
-
?
Ala-Phe + H2O
Ala + Phe
show the reaction diagram
-
-
-
-
?
Ala-Pro + H2O
Ala + Pro
show the reaction diagram
Ala-Pro-amino-4-trifluoromethylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
Ala-Pro-amino-4-trifluoromethylcoumarin + H2O
alanine + Pro-4-trifluoromethylcoumarin
show the reaction diagram
Ala-Pro-Gly + H2O
Ala + Pro-Gly
show the reaction diagram
-
-
-
?
Arg-Pro + H2O
Arg + Pro
show the reaction diagram
Asp-Pro + H2O
Asp + Pro
show the reaction diagram
-
-
-
-
?
Gly-Hyp + H2O
Gly + Hyp
show the reaction diagram
Gly-L-Pro + H2O
Gly + L-Pro
show the reaction diagram
Gly-Pro
?
show the reaction diagram
-
-
-
-
-
Gly-Pro + H2O
Gly + Pro
show the reaction diagram
Gly-Pro + H2O
Glycine + proline
show the reaction diagram
-
-
-
?
Gly-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Gly + Pro + 7-amino-4-trifluoromethylcoumarin
show the reaction diagram
-
-
-
-
?
Gly-Pro-Ala + H2O
Gly + Pro-Ala
show the reaction diagram
-
-
-
?
Gly-Pro-Gly + H2O
Gly + Pro-Gly
show the reaction diagram
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly + Pro + p-nitroaniline
show the reaction diagram
-
-
-
-
?
glycyl-L-hydroxyproline + H2O
Gly + L-hydroxyproline
show the reaction diagram
His-Pro + H2O
His + Pro
show the reaction diagram
Ile-Pro + H2O
Ile + Pro
show the reaction diagram
L-Ala-Pro + H2O
L-Ala + Pro
show the reaction diagram
L-Arg-L-Pro + H2O
L-Arg + L-Pro
show the reaction diagram
-
12.0% activity compared to L-Leu-L-Pro, in the presence of 1 mM ZnCl2
-
-
?
L-Leu-L-Pro + H2O
L-Leu + L-Pro
show the reaction diagram
L-Lys-L-Pro + H2O
L-Lys + L-Pro
show the reaction diagram
-
6.6% activity compared to L-Leu-L-Pro, in the presence of 1 mM ZnCl2
-
-
?
L-Met-L-Pro
L-Met + L-Pro
show the reaction diagram
-
-
-
-
?
L-Met-L-Pro + H2O
L-Met + L-Pro
show the reaction diagram
L-Met-Pro + H2O
L-Met + Pro
show the reaction diagram
-
-
-
-
?
L-Phe-L-Pro + H2O
L-Phe + L-Pro
show the reaction diagram
-
23.8% activity compared to L-Leu-L-Pro, in the presence of 1 mM ZnCl2
-
-
?
L-Phe-Pro + H2O
L-Phe + Pro
show the reaction diagram
L-Pro-Gly + H2O
L-Pro + Gly
show the reaction diagram
-
-
-
-
?
L-Pro-L-Ala + H2O
L-Pro + L-Ala
show the reaction diagram
-
-
-
-
?
L-Pro-L-Asp + H2O
L-Pro + L-Asp
show the reaction diagram
-
-
-
-
?
L-Pro-L-Glu + H2O
L-Pro + L-Glu
show the reaction diagram
-
-
-
-
?
L-Pro-L-Leu + H2O
L-Pro + L-Leu
show the reaction diagram
-
-
-
-
?
L-Pro-L-Met + H2O
L-Pro + L-Met
show the reaction diagram
-
-
-
-
?
L-Pro-L-Phe + H2O
L-Pro + L-Phe
show the reaction diagram
-
-
-
-
?
L-Pro-L-Ser + H2O
L-Pro + L-Ser
show the reaction diagram
-
-
-
-
?
L-Pro-L-Val + H2O
L-Pro + L-Val
show the reaction diagram
-
-
-
-
?
L-Val-L-Pro + H2O
L-Val + L-Pro
show the reaction diagram
L-Val-Pro + H2O
L-Val + Pro
show the reaction diagram
Leu-Pro + H2O
Leu + Pro
show the reaction diagram
Lys-Pro + H2O
Lys + Pro
show the reaction diagram
melphalan + H2O
?
show the reaction diagram
Met-Pro + H2O
L-Met + L-Pro
show the reaction diagram
-
68% of the activity with Gly-L-Pro
-
-
?
Met-Pro + H2O
Met + Pro
show the reaction diagram
Phe-Pro + H2O
Phe + Pro
show the reaction diagram
Pro-Ala + H2O
Pro + Ala
show the reaction diagram
Pro-Hyp + H2O
Pro + Hyp
show the reaction diagram
Pro-Pro + H2O
Pro + Pro
show the reaction diagram
prophalan-D + H2O
?
show the reaction diagram
prophalan-L + H2O
?
show the reaction diagram
Ser-Pro + H2O
Ser + Pro
show the reaction diagram
soman + H2O
?
show the reaction diagram
-
organophosphorus acid anhydrolase activity
-
-
?
Thr-Pro + H2O
Thr + Pro
show the reaction diagram
Tyr-Pro + H2O
Tyr + Pro
show the reaction diagram
-
-
-
-
?
Val-Pro + H2O
Val + Pro
show the reaction diagram
Xaa-Pro + H2O
Xaa + Pro
show the reaction diagram
-
-
?
additional information
?
-
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
Gly-Pro
?
show the reaction diagram
-
-
-
-
-
Gly-Pro + H2O
Glycine + proline
show the reaction diagram
-
-
-
?
melphalan + H2O
?
show the reaction diagram
-
prolidase-dependence of prodrug cytotoxicity in the cell lines compared to that of the parent drug, melphalan, overview
-
-
?
prophalan-D + H2O
?
show the reaction diagram
-
the D-proline prodrug of melphalan, bioactivation and uptake of prolidase-targeted proline prodrugs, prolidase-dependence of prodrug cytotoxicity in the cell lines compared to that of the parent drug, melphalan, overview
-
-
?
prophalan-L + H2O
?
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cobalt
-
2 atoms per subunit are required for optimum activity
Cu2+
activates; activates
Fe3+
-
stimulation
Na+
-
the enzyme contains five Na+ ions, four organized in two dinuclear centres and one located in an external position of the homodimer, each subunit contains two ions Na+, binding structure, overview
Ni2+
activates; activates
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2S,3R)-3-amino-2-hydroxy-5-methyl-hexanoyl-proline
-
-
(2S,3R)-3-amino-2-hydroxy-5-methylhexanoyl-proline
-
-
1,10-phenanthroline
1,2-Cylcopentanedicarboxylic acid
-
-
2-mercaptoethanol
acetic acid
-
inhibts the enzyme in colonic tissue, but not in plasma
betulinic acid
-
i.e. 3beta-hdroxy-lup-20(29)-en-28-oic acid, inhibits the enzyme and is involved in anti-angiogenesis due to further inhibition of expression and decrease in expressions of alpha1 and alpha2 integrins, hypoxia-inducible factor 1, HIF-1, and vascular endothelial cell growth factor, detailed overview
captopril
-
inhibits isozyme PD I dose-dependently, but shows no inhibition of isozyme PD II at 0.1 mM
carmustine
-
-
Colchicine
-
colchicine has a slight inhibiting effect on prolidase activity for L-Val-L-Pro, the activity reaches its highest inhibition percentage of 59% at 2.0 mM
Cupferron
-
N-Hydroxy-N-nitrosobenzeneamine ammonium salt
D,L-4-Amino-4-phosphonobutyrate
-
-
D,L-homocysteine
-
inhibits the activity at 50 mM
D,L-homocysteine-thiolactone
-
inhibits the activities of isozymes prolidase I and II in a concentration-dependent manner
daunorubicin
-
a cytotoxic anthracycline, inhibits the enzyme and collagen biosynthesis, inhibition mechanism might act via chelating of essential Mn2+ ions, more effective than doxorubicin, also inhibits DNA synthesis
dithiothreitol
DL-Ethionine
-
activates at concentrations of 1-50 mM, overview
DL-homocysteine
-
slightly activates at concentrations of 1-20 mM, inhibitory at over 30 mM, overview
DL-homocysteine thiolactone
-
activates at concentrations of 1-30 mM, inhibitory at over 50 mM, overview
DL-methionine
-
activates at concentrations of 1-30 mM, inhibitory at over 50 mM, overview
doxorubicin
-
a cytotoxic anthracycline, inhibits the enzyme and collagen biosynthesis, inhibition mechanism might act via chelating of essential Mn2+ ions, less effective than daunorubicin, also inhibits DNA synthesis
doxycyclin
-
induces down-regulation of the enzyme as a post-translational event
echistatin
-
treatment of cells results in inhibition of collagen production and enzyme activity and expression
-
Gly-PSI[CO-CH]-Pro
-
-
iodoacetamide
-
-
iodoacetate
L-isoleucine
-
inhibitory to enzyme isoform prolidase I, activating isoform prolidase II
L-Leu-L-Pro
-
-
L-leucine
-
inhibitory to enzyme isoform prolidase I, activating isoform prolidase II
L-proline
-
competitive
L-valine
-
inhibitory to enzyme isoform prolidase I, activating isoform prolidase II
L-valinyl-D-boroproline
-
-
melanin
-
30% inhibition at 0.1 mg/ml, reverses inhibition of prolidase by netilmicin
N,N'-diisopropyldiamidofluorophosphate
-
i.e. DDFP or mipafox
N-acetylproline
-
-
N-Benzyloxycarbonyl-L-proline
N-[N'-(2-bromoethyl)-N'-nitrosocarbamoyl]-L-proline
-
-
netilmicin
-
80% inhibition at 0.01 mM, reversible by melanin
p-chloromercuribenzoate
p-hydroxymercuribenzoate
paracetamol
-
mechanism of PLD inhibition by paracetamol is noncompetitive inhibition
Phenacetin
-
-
phenylacetyl-thioproline
-
-
phosphoenolpyruvate
-
-
Phosphonates
-
-
Phosphonocarboxylates
-
-
-
sodium salicylate
-
-
trans-1,2-cyclopentanedicarboxylate
-
-
Z-Pro
-
roughly 80% inhibition at 2.53 mM
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(4S)-4-ethyl-4-hydroxy-1H-pyrano[3',4':6,7]indolizino[1,2-b]quinoline-3,14(4H,12H)-dione
-
deregulates the collagen metabolism and strongly induces inhibition of collagen synthesis, but activates the enzyme accompanied by increase in the expression of b1 integrin receptor and some b1 integrin-dependent signalling proteins, e.g. Sos, MAPK ERK1and ERK2, and transcription factor NF-kB, the specific MEK/ERK inhibitor UO126 inhibits campthotecin-induced up-regulation of prolidase activity
8-Br-cGMP
-
strong and rapid stimulation of enzyme activity by phosphorylation
Acetylsalicylic acid
-
-
alpha-ketoglutarate
-
30% activation at 0.01 mM
apigenin-7-O-glucuronide
-
stimulates the enzyme and collagen biosynthesis in osteogenesis imperfecta type I cells, overview
Colchicine
-
colchicine enhances PLD activity for Gly-L-Pro and L-Leu-L-Pro, the highest enhancement of PLD on Gly-L-Pro is 141% at 0.01 mM
D,L-ethionine
-
enhances the activity of isozyme prolidase I, D,L-ethionine strongly enhances the activity of isozyme prolidase II compared with L-ethionine
D,L-homocysteine
-
enhances the activity of isozyme prolidase I at low concentration; weakly enhances the activity of isozyme prolidase II
D,L-methionine
-
slightly enhances the activity of isozyme prolidase I at low concentration; the activity of isozyme prolidase II against L-Met-L-Pro is enhanced by D,L-methionine
D-alanine
-
activation of isoforms prolidase I and prolidase II
D-Ethionine
-
enhances the activity of isozymes prolidase I and II
D-isoleucine
-
activation of isoforms prolidase I and prolidase II
D-Leucine
-
activation of isoforms prolidase I and prolidase II
D-methionine
-
the activity of isozyme prolidase I against Gly-L-Pro is strongly enhanced by D-methionine; the activity of isozyme prolidase II against L-Met-L-Pro is enhanced by D-methionine
D-serine
-
activation of isoforms prolidase I and prolidase II
D-valine
-
activation of isoforms prolidase I and prolidase II
diethyldithiocarbamate
-
activation
glycine
L-alanine
-
activation of isoforms prolidase I and prolidase II
L-ethionine
-
enhances the activity of isozyme prolidase I
L-isoleucine
-
inhibitory to enzyme isoform prolidase I, activating isoform prolidase II
L-leucine
-
inhibitory to enzyme isoform prolidase I, activating isoform prolidase II
L-methionine
-
slightly enhances the activity of isozyme prolidase I at low concentration; the activity of isozyme prolidase II against L-Met-L-Pro is enhanced by L-methionine
L-serine
-
activation of isoforms prolidase I and prolidase II
L-valine
-
inhibitory to enzyme isoform prolidase I, activating isoform prolidase II
MnCl2
-
stimulation of activity against substrates L-Pro-Gly, L-Pro-L-Glu, L-Pro-L-Leu, L-Pro-L-Ser, and L-Pro-L-Phe, inhibitory to hydrolysis of substrates L-Pro-L-Ala, L-Pro-L-Val, L-Pro-L-Met, and L-Pro-L-Asp
N-[N'-(2-bromoethyl)-N'-nitrosocarbamoyl]-L-proline
-
significantly increases MCF-7 cells prolidase activity, when used at 0.05-0.25 mM concentrations
N-[N'-(2-chloroethyl)-N'-nitrosocarbamoyl]-L-proline
-
significantly increases MCF-7 cells prolidase activity, when used at 0.05-0.25 mM concentrations
-
N-[N'-(3-chloropropyl)-N'-nitrosocarbamoyl]-L-proline
-
significantly increases MCF-7 cells prolidase activity, when used at 0.05-0.25 mM concentrations
-
N-[N'-(4-bromophenyl)-N'-nitrosocarbamoyl]-L-proline
-
significantly increases MCF-7 cells prolidase activity, when used at 0.05-0.25 mM concentrations
-
pectolinarin
-
stimulates the enzyme and collagen biosynthesis in osteogenesis imperfecta type I cells, overview
thrombin
-
treatment of cells results in enhancement of collagen production and enzyme activity and expression, accompanied by raise in expression of focal adhesion kinase pp125 and mitogen-activated protein kinases
-
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.127 - 8.3
Ala-Pro
6.7
Gly-Hyp
-
-
1.64 - 6.23
Gly-L-Pro
0.006 - 7.1
Gly-Pro
0.39
His-Pro
-
-
0.395 - 23.3
L-Leu-L-Pro
4.11 - 9.89
L-Met-L-Pro
6.8 - 26.9
L-Pro-Gly
4.2 - 19.1
L-Pro-L-Met
3.2 - 28.6
L-Pro-L-Val
0.243 - 0.269
L-Val-L-Pro
0.2 - 10.4
Leu-Pro
0.81 - 14.5
Met-Pro
0.76 - 25
Phe-Pro
12.5
Pro-Hyp
-
-
0.38
Pro-Pro
-
-
0.06 - 4.2
Val-Pro
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 22
Ala-Pro
683
Gly-Pro
Homo sapiens
-
-
55.3
Ile-Pro
Cavia porcellus
-
-
109
L-Met-L-Pro
Escherichia coli
-
-
111 - 2861
Leu-Pro
115 - 7481
Met-Pro
additional information
additional information
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
980 - 2049
Leu-Pro
13 - 2006
Met-Pro
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15.3
L-Leu-L-Pro
-
wild type enzyme, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50C
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
captopril
Rattus norvegicus
-
isozyme PD I, pH 7.8, 37C
0.038
carmustine
Sus scrofa
-
in 0.05 M Tris-HCl, pH 7.8, 2 mM MnCl2, at 37C
0.005
N-Benzyloxycarbonyl-L-proline
Rattus norvegicus
-
isozyme PD I, pH 7.8, 37C
0.082
N-[N'-(2-bromoethyl)-N'-nitrosocarbamoyl]-L-proline
Sus scrofa
-
in 0.05 M Tris-HCl, pH 7.8, 2 mM MnCl2, at 37C
0.005
netilmicin
Homo sapiens
-
-
0.05
Ni2+
Rattus norvegicus
-
isozyme PD II, pH 7.8, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000059
-
substrate prophalan-L
0.024
-
PepX, cell extract
0.041
-
PepQ, cell extract
0.129
-
PepI, cell extract
0.33
-
mutant enzyme S307R, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50C
0.48
-
mutant enzyme S307D, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50C
0.64
-
mutant enzyme R293S, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50C
0.67
-
mutant H284A, pH 7.0, 100C
0.73
-
mutant H284L, pH 7.0, 100C
1.02
-
mutant D209A, pH 7.0, 100C
1.1
-
mutant enzyme S307D, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50C
1.4
-
mutant enzyme R293S, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50C; mutant enzyme S307D, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50C
1.7
-
mutant enzyme S307D, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50C
2
-
mutant enzyme R293S, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50C
2.7
-
mutant enzyme S307D, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50C
3 - 3.9
-
mutant enzyme R293S/S307G, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50C
3.2
-
mutant enzyme R293S, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50C; mutant enzyme S307D, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50C
4.3
-
mutant enzyme R293S, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50C
4.4
-
mutant enzyme S307G, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50C
4.8
-
mutant enzyme R293S, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50C
5
-
mutant enzyme R293S, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50C
5.2
-
mutant enzyme S307D, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50C
5.3
-
mutant enzyme R293S, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50C
5.632
-
37C, pH 7.8, dipeptidase activity
5.9
-
mutant enzyme R293S, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50C
6.2
-
mutant enzyme S307R, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50C
7
-
mutant enzyme R293S/S307G, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50C
7.8
-
mutant enzyme S307G, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50C
8.2
-
mutant enzyme S307R, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50C
8.9
-
mutant enzyme S307R, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50C
9.6
-
mutant enzyme S307G, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50C; mutant enzyme S307G, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50C
10
-
at 30C, with organophosphorus compound substrate diisopropyl phosphorofluoridate, DFP
10.6
-
mutant enzyme S307R, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50C
11.6
-
mutant enzyme S307D, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50C
11.9
-
mutant enzyme S307R, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50C
12.4
-
mutant enzyme S307G, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50C
12.8
-
mutant enzyme S307G, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50C
13.3
prolidase in presence of 10 mM Zn2+
13.4
-
mutant enzyme R293S/S307G, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50C
13.6
-
mutant enzyme R293S/S307G, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50C
18.4
-
mutant enzyme S307R, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50C
22.7
-
mutant enzyme R293S/S307G, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50C
25.6
-
mutant enzyme S307D, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50C
27.3
-
wild type enzyme, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50C
27.6
-
mutant enzyme R293S/S307G, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50C
30
-
at 55C, with organophosphorus compound substrate diisopropyl phosphorofluoridate, DFP
30.9
-
wild type enzyme, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50C
31.5
-
mutant enzyme S307D, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50C
32.3
-
mutant enzyme R293S/S307G, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50C
32.7
-
mutant enzyme S307G, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50C
36.9
-
mutant enzyme S307G, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50C
42.3
-
mutant enzyme S307R, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50C
46.7
-
mutant enzyme R293S/S307G, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50C
48.3
-
mutant enzyme R293S/S307G, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50C
53.7
-
mutant enzyme S307G, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50C
56.2
-
wild type enzyme, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50C
64.9
-
mutant enzyme R293S, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50C
67.7
-
wild type enzyme, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50C
78.2
-
mutant enzyme R293S/S307G, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50C
81.8
-
mutant enzyme S307G, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50C
87.8
-
mutant enzyme S307R, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50C
100.8
-
mutant enzyme S307R, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50C
111.4
-
wild type enzyme, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50C
158.3
prolidase in presence of 10 mM Mn2+
159.7
-
wild type enzyme, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50C
166.1
-
wild type enzyme, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50C
197.2
purified recombinant enzyme
223
-
-
226.5
-
cell lystae supernatant, pH 7.8, 37C
234.5
-
wild type enzyme, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50C
463.7
-
wild type enzyme, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50C
468.7
-
wild type enzyme, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50C
590
-
purified crystallized recombinant enzyme
630
-
native enzyme
809
substratwe: Leu-Pro, pH 7.0, 70C, wild-type enzyme
1119
substrate: Leu-Pro, pH 7.0, 70C, mutant enzyme E127G/E252D
1245
substrate: Leu-Pro, pH 7.0, 70C, mutant enzyme A195T/G306S
1300
-
purified noncrystallized recombinant enzyme
1360
-
recombinant enzyme
1388
-
wild-type, pH 7.0, 100C
1597
substrate: Leu-Pro, pH 7.0, 70C, mutant enzyme E36V
1938
purified recombinant enzyme, 100C, substrate Met-Pro
2000
-
-
2146
substrate: Leu-Pro, pH 7.0, 70C, mutant enzyme Y301C/K342N
2355
purified recombinant enzyme, 100C, substrate Met-Pro
21500
-
pH 7.8, 37C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
dipeptidase activity, 20% of maximum activity
6.5 - 7.5
-
-
6.5
-
wild-type enzyme
6.8
-
substrate Ala-Pro
7.25 - 7.5
-
prolidase I
7.5 - 8
-
prolidase II
7.6 - 9
-
Tris-HCl buffer
7.6
-
assay at
7.8 - 8
-
assay at
7.8 - 8
-
assay at
10
-
dipeptidase activity, 80% of maximum activity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8.5
-
activity profiles of wild-type and mutant enzymes, overview
4 - 10
5 - 7.5
-
-
5.5 - 8.6
-
less than 10% activity below and above
6 - 8
pH profile, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 100
-
activities of wild-type and mutant enzymes at 100C
37 - 50
-
native enzyme
60
-
temperature optimum of the mutant enzymes L193R, V302D, and L193T
70
-
temperature optimum of the mutant enzymes L193E/V302D and L193R/V302D, the wild-type enzyme is inactive
80 - 100
assay at; assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 60
67% of maximal activity at 60C, no activity at 70C
35 - 100
-
highest activities of wild-type and mutant enzymes at 100C
37 - 50
-
50% of maximal activity at 37C
50 - 100
-
hardly active below 50C, optimal activity at 100C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
from pregenancies with healthy fetusses and those with neural tube defect
Manually annotated by BRENDA team
-
enzyme activity is increased in aortic dilatation compared to controls
Manually annotated by BRENDA team
-
increased PSR activity in case of colitis
Manually annotated by BRENDA team
-
prolidase activity is increased in ovarian cancer, overview
Manually annotated by BRENDA team
-
high activity
Manually annotated by BRENDA team
-
prolidase is down-regulated in lymphoma samples
Manually annotated by BRENDA team
-
fibroblast cell line
Manually annotated by BRENDA team
-
from healthy individuals and from tuberculous pleurisy patients, 19.1fold elevated pleural fluid and serum prolidase enzyme activity in patients with tuberculosis pleurisy compared with non-tuberculosis pleurisy group