Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
2146
substrate: Leu-Pro, pH 7.0, 70°C, mutant enzyme Y301C/K342N
22.7
-
mutant enzyme R293S/S307G, in the presence of 1 mM MnCl2, using L-Leu-L-Pro as substrate, at 50°C
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
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
1.4
-
mutant enzyme R293S, in the presence of 1 mM ZnCl2, using L-Phe-L-Pro as substrate, at 50°C
1.4
-
mutant enzyme S307D, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50°C
3.2
-
mutant enzyme R293S, in the presence of 1 mM ZnCl2, using L-Lys-L-Pro as substrate, at 50°C
3.2
-
mutant enzyme S307D, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50°C
9.6
-
mutant enzyme S307G, in the presence of 1 mM MnCl2, using L-Lys-L-Pro as substrate, at 50°C
9.6
-
mutant enzyme S307G, in the presence of 1 mM MnCl2, using L-Phe-L-Pro as substrate, at 50°C
additional information
-
activities of strain JD6.5 enzyme in the presence or absence of various biodegradeable and water-soluble wetting agents, degreasers, or foams, overview
additional information
-
-
additional information
-
-
additional information
-
assay method development and evaluation, capillary electrophoresis with Ru(bpy)3 2+ electrochemiluminescence detection, overview
additional information
-
cord blood prolidase activity is 41.4 U/l in term infants and 35.2 U/l in preterm infants
additional information
-
serum prolidase is 952 U/l in patients with pleural tuberculosis
additional information
-
specific activities with melphalan and prodrugs in cancer cell lines, overview
additional information
-
1412 U/l in epithelial ovarian cancer compred to 1338 U/l in controls
additional information
-
45.7 U/l for control group, 53.5 U/l for patients with erectile dysfunction
additional information
-
prolidase activity in correlation to aorta diameter, overview
additional information
-
-
additional information
-
-
additional information
substrate and metal specificities, recombinant enzyme, overview
additional information
substrate and metal specificities, recombinant enzyme, overview
additional information
substrate and metal specificities, recombinant enzyme, overview
additional information
-
substrate and metal specificities, recombinant enzyme, overview
additional information
-
overall tissue-specific prolidase activity in brain regions with different substrates