3.4.13.9: Xaa-Pro dipeptidase
This is an abbreviated version!
For detailed information about Xaa-Pro dipeptidase, go to the full flat file.
Word Map on EC 3.4.13.9
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3.4.13.9
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collagen
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dipeptides
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ulcer
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hydroxyproline
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gly-pro
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opaas
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soman
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exopeptidase
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proline-containing
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prolinase
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map-kinases
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paraoxonase
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dfp
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igf-ir
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alteromonas
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erk1
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splenomegaly
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sarin
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medicine
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beta1-integrin
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analysis
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diagnostics
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drug development
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degradation
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biotechnology
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food industry
- 3.4.13.9
- collagen
- dipeptides
- ulcer
- hydroxyproline
- gly-pro
-
opaas
- soman
-
exopeptidase
-
proline-containing
- prolinase
-
map-kinases
- paraoxonase
- dfp
- igf-ir
- alteromonas
- erk1
-
splenomegaly
- sarin
- medicine
- beta1-integrin
- analysis
- diagnostics
- drug development
- degradation
- biotechnology
- food industry
Reaction
hydrolysis of Xaa-/-Pro dipeptides; also acts on aminoacyl-hydroxyamine analogues. No action on Pro-Pro =
Synonyms
clan MG aminopeptidase P-like metallopeptidase, dipeptidase, proline, DPP8, EC 3.4.3.7, gamma-peptidase, imidodipeptidase, LGAS_0712, M24B peptidase, More, MP50, OPAA, OPAA-2, organophosphate acid anhydrolase, organophosphate anhydrolase/prolidase, organophosphorus acid anhydrolase, PepD, PepE, PepI, PepQ, peptidase D, peptidase-Q, PepX, Pf-peptidase, Pfprol, PH0974, PH1149, Ph1prol, Phprol, PLD, post-proline-cleaving aminopeptidase, prolidase, prolidase homolog 1, prolidase homolog 2, prolidase I, prolidase II, Proline dipeptidase, proline iminopeptidase, proline-specific amino dipeptidase, prolyl dipeptidase, PRS, QPP, quiescent cell proline dipeptidase, serum prolidase, X-Pro dipeptidase, X-prolyl-dipeptidyl aminopeptidase, Xaa-Pro dipeptidase, XPD, XPD43, XPP
ECTree
3.4.13.9 Xaa-Pro dipeptidaseAdvanced search results
results (
results (KM Value
KM Value on EC 3.4.13.9 - Xaa-Pro dipeptidase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
2.13
Gly-L-Pro
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in the presence of 0.1 mM colchicine, 1.0 mM Mn2+, in 30 mM phosphate buffer (pH 7.5) 5.0 mM Ru(bpy)32+, at 37°C
6.23
Gly-L-Pro
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in the absence of colchicine, 1.0 mM Mn2+, in 30 mM phosphate buffer (pH 7.5) 5.0 mM Ru(bpy)32+, at 37°C
2.88 - 2.9
Gly-Pro
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prolidase I from normal human and mother of patient with prolidase deficiency
0.395
L-Leu-L-Pro
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in the presence of 0.1 mM colchicine, 1.0 mM Mn2+, in 30 mM phosphate buffer (pH 7.5) 5.0 mM Ru(bpy)32+, at 37°C
0.628
L-Leu-L-Pro
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in the absence of colchicine, 1.0 mM Mn2+, in 30 mM phosphate buffer (pH 7.5) 5.0 mM Ru(bpy)32+, at 37°C
1.7
L-Leu-L-Pro
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mutant enzyme S307G, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C
8
L-Leu-L-Pro
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wild type enzyme, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C
10.1
L-Leu-L-Pro
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mutant enzyme R293S/S307G, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C
14.7
L-Leu-L-Pro
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mutant enzyme S307R, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C
18
L-Leu-L-Pro
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mutant enzyme S307D, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C
23.3
L-Leu-L-Pro
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mutant enzyme R293S, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C
4.43
L-Met-L-Pro
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pH 7.8, 37°C, presence of 20 mM glycine, enzyme from patient with enzyme deficiency
5.48
L-Met-L-Pro
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pH 7.8, 37°C, presence of 20 mM L-valine, enzyme from patient with enzyme deficiency
6.16
L-Met-L-Pro
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pH 7.8, 37°C, presence of 20 mM D-valine, enzyme from patient with enzyme deficiency
8.6
L-Pro-Gly
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pH 7.8, 37°C, presence of 0.1 mM MnCl2 plus 20 mM glycine, enzyme from patient with enzyme deficiency
9.7
L-Pro-Gly
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pH 7.8, 37°C, presence of 0.1 mM MnCl2, enzyme from patient with enzyme deficiency
16.7
L-Pro-Gly
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pH 7.8, 37°C, presence of 20 mM glycine, enzyme from patient with enzyme deficiency
4.2
L-Pro-L-Met
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pH 7.8, 37°C, presence of 20 mM glycine, enzyme from patient with enzyme deficiency
5
L-Pro-L-Met
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pH 7.8, 37°C, presence of 0.1 mM MnCl2 plus 20 mM glycine, enzyme from patient with enzyme deficiency
9.7
L-Pro-L-Met
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pH 7.8, 37°C, presence of 0.1 mM MnCl2, enzyme from patient with enzyme deficiency
3.2
L-Pro-L-Val
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pH 7.8, 37°C, presence of 20 mM glycine, enzyme from patient with enzyme deficiency
5.5
L-Pro-L-Val
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pH 7.8, 37°C, presence of 0.1 mM MnCl2 plus 20 mM glycine, enzyme from patient with enzyme deficiency
10.1
L-Pro-L-Val
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pH 7.8, 37°C, presence of 0.1 mM MnCl2, enzyme from patient with enzyme deficiency
0.243
L-Val-L-Pro
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in the presence of 0.1 mM colchicine, 1.0 mM Mn2+, in 30 mM phosphate buffer (pH 7.5) 5.0 mM Ru(bpy)32+, at 37°C
0.269
L-Val-L-Pro
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in the absence of colchicine, 1.0 mM Mn2+, in 30 mM phosphate buffer (pH 7.5) 5.0 mM Ru(bpy)32+, at 37°C
11.1
Met-Pro
pH 7.0, 100°C, recombinant mutant R19G/G39E/K71E/S229T
additional information
additional information
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kinetics of wild-type and mutant enzymes
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additional information
additional information
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kinetics and substrate specificity of wild-type and mutant enzymes, overview
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additional information
additional information
the recombinant enzyme shows an allosteric behaviour, overview
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