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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

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 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.13 Dipeptidases
                3.4.13.9 Xaa-Pro dipeptidase

Specific Activity

Specific Activity on EC 3.4.13.9 - Xaa-Pro dipeptidase

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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 50°C
0.48
-
mutant enzyme S307D, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50°C
0.64
-
mutant enzyme R293S, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50°C
0.67
-
mutant H284A, pH 7.0, 100°C
0.73
-
mutant H284L, pH 7.0, 100°C
1.02
-
mutant D209A, pH 7.0, 100°C
1.1
-
mutant enzyme S307D, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50°C
1.7
-
mutant enzyme S307D, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50°C
10
-
at 30°C, 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 50°C
100.8
-
mutant enzyme S307R, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50°C
11.6
-
mutant enzyme S307D, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50°C
11.9
-
mutant enzyme S307R, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50°C
111.4
-
wild type enzyme, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50°C
1119
substrate: Leu-Pro, pH 7.0, 70°C, mutant enzyme E127G/E252D
12.4
-
mutant enzyme S307G, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50°C
12.8
-
mutant enzyme S307G, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50°C
1245
substrate: Leu-Pro, pH 7.0, 70°C, mutant enzyme A195T/G306S
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 50°C
13.6
-
mutant enzyme R293S/S307G, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50°C
1300
purified noncrystallized recombinant enzyme
1360
-
recombinant enzyme
1388
-
wild-type, pH 7.0, 100°C
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 50°C
1597
substrate: Leu-Pro, pH 7.0, 70°C, mutant enzyme E36V
166.1
-
wild type enzyme, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50°C
18.4
-
mutant enzyme S307R, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50°C
1938
purified recombinant enzyme, 100°C, substrate Met-Pro
197.2
purified recombinant enzyme
2
-
mutant enzyme R293S, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50°C
2.7
-
mutant enzyme S307D, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50°C
2000
-
-
2146
substrate: Leu-Pro, pH 7.0, 70°C, mutant enzyme Y301C/K342N
21500
-
pH 7.8, 37°C
22.7
-
mutant enzyme R293S/S307G, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50°C
223
-
-
226.5
-
cell lystae supernatant, pH 7.8, 37°C
234.5
-
wild type enzyme, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50°C
2355
purified recombinant enzyme, 100°C, substrate Met-Pro
25.6
-
mutant enzyme S307D, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50°C
27.3
-
wild type enzyme, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50°C
27.6
-
mutant enzyme R293S/S307G, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50°C
3 - 3.9
-
mutant enzyme R293S/S307G, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50°C
30
-
at 55°C, 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 50°C
31.5
-
mutant enzyme S307D, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50°C
32.3
-
mutant enzyme R293S/S307G, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50°C
32.7
-
mutant enzyme S307G, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50°C
36.9
-
mutant enzyme S307G, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50°C
4.3
-
mutant enzyme R293S, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50°C
4.4
-
mutant enzyme S307G, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50°C
4.8
-
mutant enzyme R293S, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50°C
42.3
-
mutant enzyme S307R, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50°C
46.7
-
mutant enzyme R293S/S307G, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50°C
463.7
-
wild type enzyme, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50°C
468.7
-
wild type enzyme, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50°C
48.3
-
mutant enzyme R293S/S307G, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50°C
5
-
mutant enzyme R293S, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50°C
5.2
-
mutant enzyme S307D, in the presence of 1 mM MnCl2, using L-Val-L-Pro as substrate, at 50°C
5.3
-
mutant enzyme R293S, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50°C
5.632
-
37°C, 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 50°C
53.7
-
mutant enzyme S307G, in the presence of 1 mM MnCl2, using L-Arg-L-Pro as substrate, at 50°C
56.2
-
wild type enzyme, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50°C
590
purified crystallized recombinant enzyme
6.2
-
mutant enzyme S307R, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50°C
630
-
native enzyme
64.9
-
mutant enzyme R293S, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50°C
67.7
-
wild type enzyme, in the presence of 1 mM ZnCl2, using L-Val-L-Pro as substrate, at 50°C
7
-
mutant enzyme R293S/S307G, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50°C
7.8
-
mutant enzyme S307G, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50°C
78.2
-
mutant enzyme R293S/S307G, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50°C
8.2
-
mutant enzyme S307R, in the presence of 1 mM ZnCl2, using L-Arg-L-Pro as substrate, at 50°C
8.9
-
mutant enzyme S307R, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50°C
809
substratwe: Leu-Pro, pH 7.0, 70°C, wild-type enzyme
81.8
-
mutant enzyme S307G, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50°C
87.8
-
mutant enzyme S307R, in the presence of 1 mM ZnCl2, using L-Leu-L-Pro as substrate, at 50°C
additional information