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4-nitrophenyl soman + H2O
?
-
-
-
?
Ala-Ala + H2O
Ala + Ala
-
-
-
-
?
Ala-Phe + H2O
Ala + Phe
-
-
-
-
?
Ala-Pro-amino-4-trifluoromethylcoumarin + H2O
?
-
-
-
?
Ala-Pro-amino-4-trifluoromethylcoumarin + H2O
alanine + Pro-4-trifluoromethylcoumarin
Ala-Pro-Gly + H2O
Ala + Pro-Gly
Asp-Pro + H2O
Asp + Pro
-
-
-
-
?
Gly-L-Pro + H2O
Gly + L-Pro
Gly-Pro + H2O
Glycine + proline
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly + Pro-4-nitroanilide
Gly-Pro-4-trifluoromethylcoumarin-7-amide + H2O
Gly + Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
Gly-Pro-Ala + H2O
Gly + Pro-Ala
Gly-Pro-Gly + H2O
Gly + Pro-Gly
Gly-Pro-p-nitroanilide + H2O
Gly + Pro + p-nitroaniline
-
-
-
-
?
glycyl-L-hydroxyproline + H2O
Gly + L-hydroxyproline
L-Ala-L-Pro + H2O
L-Ala + L-Pro
-
-
-
-
?
L-Ala-Pro + H2O
L-Ala + Pro
L-Arg-L-Pro + H2O
L-Arg + L-Pro
-
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
L-Lys-L-Pro + H2O
L-Lys + L-Pro
-
6.6% activity compared to L-Leu-L-Pro, in the presence of 1 mM ZnCl2
-
-
?
L-Met-L-Pro
L-Met + L-Pro
-
-
-
-
?
L-Met-L-Pro + H2O
L-Met + L-Pro
L-Met-Pro + H2O
L-Met + Pro
-
-
-
-
?
L-Phe-L-Pro + H2O
L-Phe + L-Pro
L-Phe-Pro + H2O
L-Phe + Pro
L-Pro-Gly + H2O
L-Pro + Gly
-
-
-
-
?
L-Pro-L-Ala + H2O
L-Pro + L-Ala
-
-
-
-
?
L-Pro-L-Asp + H2O
L-Pro + L-Asp
-
-
-
-
?
L-Pro-L-Glu + H2O
L-Pro + L-Glu
-
-
-
-
?
L-Pro-L-Leu + H2O
L-Pro + L-Leu
-
-
-
-
?
L-Pro-L-Met + H2O
L-Pro + L-Met
-
-
-
-
?
L-Pro-L-Phe + H2O
L-Pro + L-Phe
-
-
-
-
?
L-Pro-L-Ser + H2O
L-Pro + L-Ser
-
-
-
-
?
L-Pro-L-Val + H2O
L-Pro + L-Val
-
-
-
-
?
L-Val-L-Pro + H2O
L-Val + L-Pro
L-Val-Pro + H2O
L-Val + Pro
Met-Ala-Ala + H2O
Met + Ala-Ala
Met-Pro + H2O
L-Met + L-Pro
-
68% of the activity with Gly-L-Pro
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
Phe-Pro-Gly-Pro-Ile + H2O
Phe + Pro-Gly-Pro-Ile
soman + H2O
?
-
organophosphorus acid anhydrolase activity
-
-
?
Tyr-Pro-Phe-Pro-Gly-Pro-Ile + H2O
Tyr + Pro-Phe-Pro-Gly-Pro-Ile
Xaa-Pro + H2O
Xaa + Pro
-
-
?
additional information
?
-
Ala-Pro + H2O
Ala + Pro
-
-
-
-
?
Ala-Pro + H2O
Ala + Pro
-
enzyme-substrate interaction model
-
-
?
Ala-Pro + H2O
Ala + Pro
-
-
-
?
Ala-Pro + H2O
Ala + Pro
-
-
-
?
Ala-Pro + H2O
Ala + Pro
-
-
-
?
Ala-Pro + H2O
Ala + Pro
-
preferred substrate of isozyme PD I
-
-
?
Ala-Pro + H2O
Ala + Pro
-
best substrate of isozyme PD I
-
-
?
Ala-Pro-amino-4-trifluoromethylcoumarin + H2O
alanine + Pro-4-trifluoromethylcoumarin
-
-
-
?
Ala-Pro-amino-4-trifluoromethylcoumarin + H2O
alanine + Pro-4-trifluoromethylcoumarin
-
-
-
?
Ala-Pro-Gly + H2O
Ala + Pro-Gly
-
-
-
?
Ala-Pro-Gly + H2O
Ala + Pro-Gly
-
-
-
?
Arg-Pro + H2O
Arg + Pro
-
preferred substrate
-
-
?
Arg-Pro + H2O
Arg + Pro
-
-
-
-
?
Arg-Pro + H2O
Arg + Pro
-
-
-
-
?
Arg-Pro + H2O
Arg + Pro
the substrate Leu-Pro is preferred with cofactor zinc, whereas Arg-Pro is preferred with manganese, the enzyme shows an allosteric response to changes in substrate concentrations, with a Hill constant of 1.57 for Arg-Pro
-
-
?
Arg-Pro + H2O
Arg + Pro
the substrate Leu-Pro is preferred with cofactor zinc, whereas Arg-Pro is preferred with manganese, the enzyme shows an allosteric response to changes in substrate concentrations, with a Hill constant of 1.57 for Arg-Pro
-
-
?
Arg-Pro + H2O
Arg + Pro
-
-
-
?
Arg-Pro + H2O
Arg + Pro
-
-
-
?
Arg-Pro + H2O
Arg + Pro
-
-
-
?
Arg-Pro + H2O
Arg + Pro
-
-
-
?
Arg-Pro + H2O
Arg + Pro
-
-
-
?
Gly-Hyp + H2O
Gly + Hyp
-
-
-
-
?
Gly-Hyp + H2O
Gly + Hyp
-
-
-
-
?
Gly-L-Pro + H2O
Gly + L-Pro
-
-
-
-
?
Gly-L-Pro + H2O
Gly + L-Pro
-
-
-
-
?
Gly-L-Pro + H2O
Gly + L-Pro
-
-
667109, 667350, 667803, 668271, 668292, 670953, 695528, 695908, 697476, 697568, 697758, 699153, 699184, 700612, 710614 -
-
?
Gly-L-Pro + H2O
Gly + L-Pro
-
-
-
-
?
Gly-L-Pro + H2O
Gly + L-Pro
-
-
-
-
?
Gly-L-Pro + H2O
Gly + L-Pro
-
-
-
-
?
Gly-L-Pro + H2O
Gly + L-Pro
-
-
-
-
?
Gly-Pro + H2O
Gly + Pro
-
-
-
-
?
Gly-Pro + H2O
Gly + Pro
-
-
-
-
?
Gly-Pro + H2O
Gly + Pro
-
-
-
?
Gly-Pro + H2O
Gly + Pro
-
-
-
?
Gly-Pro + H2O
Gly + Pro
-
-
-
-
?
Gly-Pro + H2O
Gly + Pro
-
-
-
-
r
Gly-Pro + H2O
Gly + Pro
-
preferred substrate
-
-
?
Gly-Pro + H2O
Gly + Pro
-
prolidase I activity
-
-
?
Gly-Pro + H2O
Gly + Pro
-
assay at pH 8.0, 37°C
-
-
?
Gly-Pro + H2O
Gly + Pro
-
-
-
-
?
Gly-Pro + H2O
Gly + Pro
-
-
-
-
?
Gly-Pro + H2O
Gly + Pro
-
-
-
?
Gly-Pro + H2O
Gly + Pro
-
-
-
?
Gly-Pro + H2O
Gly + Pro
-
-
-
?
Gly-Pro + H2O
Gly + Pro
-
-
-
?
Gly-Pro + H2O
Gly + Pro
-
-
-
-
?
Gly-Pro + H2O
Gly + Pro
-
very low activity with isozyme PD II
-
-
?
Gly-Pro + H2O
Gly + Pro
-
-
-
-
?
Gly-Pro + H2O
Gly + Pro
-
-
-
ir
Gly-Pro + H2O
Gly + Pro
-
-
-
ir
Gly-Pro + H2O
Gly + Pro
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly + Pro-4-nitroanilide
-
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly + Pro-4-nitroanilide
-
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly + Pro-4-nitroanilide
-
-
-
-
?
Gly-Pro-Ala + H2O
Gly + Pro-Ala
-
-
-
?
Gly-Pro-Ala + H2O
Gly + Pro-Ala
-
-
-
?
Gly-Pro-Gly + H2O
Gly + Pro-Gly
-
-
-
?
Gly-Pro-Gly + H2O
Gly + Pro-Gly
-
-
-
?
glycyl-L-hydroxyproline + H2O
Gly + L-hydroxyproline
-
-
-
-
?
glycyl-L-hydroxyproline + H2O
Gly + L-hydroxyproline
-
-
-
-
?
His-Pro + H2O
His + Pro
-
-
-
-
?
His-Pro + H2O
His + Pro
-
-
-
-
?
His-Pro + H2O
His + Pro
-
-
-
?
Ile-Pro + H2O
Ile + Pro
-
-
-
-
?
Ile-Pro + H2O
Ile + Pro
-
-
-
-
?
Ile-Pro + H2O
Ile + Pro
-
-
-
-
?
Ile-Pro + H2O
Ile + Pro
-
-
-
-
?
L-Ala-Pro + H2O
L-Ala + Pro
-
-
-
-
?
L-Ala-Pro + H2O
L-Ala + Pro
-
-
-
-
?
L-Ala-Pro + H2O
L-Ala + Pro
-
-
-
-
?
L-Ala-Pro + H2O
L-Ala + Pro
-
-
-
-
?
L-Ala-Pro + H2O
L-Ala + Pro
-
-
-
-
?
L-Ala-Pro + H2O
L-Ala + Pro
-
-
-
-
?
L-Ala-Pro + H2O
L-Ala + Pro
-
-
-
-
?
L-Ala-Pro + H2O
L-Ala + Pro
-
-
-
-
?
L-Leu-L-Pro + H2O
L-Leu + L-Pro
-
-
-
-
?
L-Leu-L-Pro + H2O
L-Leu + L-Pro
-
-
-
-
?
L-Leu-L-Pro + H2O
L-Leu + L-Pro
-
100% activity in the presence of 1 mM ZnCl2
-
-
?
L-Met-L-Pro + H2O
L-Met + L-Pro
-
-
-
-
?
L-Met-L-Pro + H2O
L-Met + L-Pro
-
-
-
-
?
L-Met-L-Pro + H2O
L-Met + L-Pro
-
-
-
-
?
L-Met-L-Pro + H2O
L-Met + L-Pro
-
-
-
-
?
L-Phe-L-Pro + H2O
L-Phe + L-Pro
-
-
-
-
?
L-Phe-L-Pro + H2O
L-Phe + L-Pro
-
23.8% activity compared to L-Leu-L-Pro, in the presence of 1 mM ZnCl2
-
-
?
L-Phe-Pro + H2O
L-Phe + Pro
-
-
-
-
?
L-Phe-Pro + H2O
L-Phe + Pro
-
-
-
-
?
L-Phe-Pro + H2O
L-Phe + Pro
-
-
-
-
?
L-Phe-Pro + H2O
L-Phe + Pro
-
prolidase II activity
-
-
?
L-Phe-Pro + H2O
L-Phe + Pro
-
-
-
-
?
L-Phe-Pro + H2O
L-Phe + Pro
-
-
-
-
?
L-Phe-Pro + H2O
L-Phe + Pro
-
-
-
-
?
L-Phe-Pro + H2O
L-Phe + Pro
-
-
-
-
?
L-Phe-Pro + H2O
L-Phe + Pro
-
-
-
-
?
L-Phe-Pro + H2O
L-Phe + Pro
-
specific for active bond in trans configuration
-
-
?
L-Val-L-Pro + H2O
L-Val + L-Pro
-
-
-
-
?
L-Val-L-Pro + H2O
L-Val + L-Pro
-
-
-
-
?
L-Val-L-Pro + H2O
L-Val + L-Pro
-
14.4% activity compared to L-Leu-L-Pro, in the presence of 1 mM ZnCl2
-
-
?
L-Val-L-Pro + H2O
L-Val + L-Pro
-
-
-
-
?
L-Val-Pro + H2O
L-Val + Pro
-
-
-
-
?
L-Val-Pro + H2O
L-Val + Pro
-
-
-
-
?
L-Val-Pro + H2O
L-Val + Pro
-
-
-
-
?
L-Val-Pro + H2O
L-Val + Pro
-
-
-
-
?
L-Val-Pro + H2O
L-Val + Pro
-
-
-
-
?
Leu-Pro + H2O
Leu + Pro
-
-
-
-
?
Leu-Pro + H2O
Leu + Pro
-
-
-
-
?
Leu-Pro + H2O
Leu + Pro
-
-
-
-
?
Leu-Pro + H2O
Leu + Pro
-
-
-
-
?
Leu-Pro + H2O
Leu + Pro
-
-
-
-
?
Leu-Pro + H2O
Leu + Pro
-
-
-
-
?
Leu-Pro + H2O
Leu + Pro
-
-
-
-
?
Leu-Pro + H2O
Leu + Pro
-
-
-
-
?
Leu-Pro + H2O
Leu + Pro
-
-
-
-
?
Leu-Pro + H2O
Leu + Pro
the substrate Leu-Pro is preferred with cofactor zinc, whereas Arg-Pro is preferred with manganese, the enzyme shows an allosteric response to changes in substrate concentrations, with a Hill constant of 1.53 for Leu-Pro
-
-
?
Leu-Pro + H2O
Leu + Pro
the substrate Leu-Pro is preferred with cofactor zinc, whereas Arg-Pro is preferred with manganese, the enzyme shows an allosteric response to changes in substrate concentrations, with a Hill constant of 1.53 for Leu-Pro
-
-
?
Leu-Pro + H2O
Leu + Pro
-
-
-
-
?
Leu-Pro + H2O
Leu + Pro
best substrate
-
-
?
Leu-Pro + H2O
Leu + Pro
best substrate
-
-
?
Leu-Pro + H2O
Leu + Pro
-
-
-
-
?
Leu-Pro + H2O
Leu + Pro
-
-
-
?
Leu-Pro + H2O
Leu + Pro
-
-
-
?
Leu-Pro + H2O
Leu + Pro
high activity
-
-
?
Leu-Pro + H2O
Leu + Pro
high activity
-
-
?
Leu-Pro + H2O
Leu + Pro
-
-
-
?
Leu-Pro + H2O
Leu + Pro
-
-
-
-
?
Leu-Pro + H2O
Leu + Pro
-
-
-
?
Leu-Pro + H2O
Leu + Pro
-
-
-
?
Lys-Pro + H2O
Lys + Pro
-
-
-
-
?
Lys-Pro + H2O
Lys + Pro
-
-
-
-
?
Lys-Pro + H2O
Lys + Pro
-
-
-
-
?
Lys-Pro + H2O
Lys + Pro
-
-
-
?
Lys-Pro + H2O
Lys + Pro
-
-
-
?
melphalan + H2O
?
-
-
-
-
?
melphalan + H2O
?
-
prolidase-dependence of prodrug cytotoxicity in the cell lines compared to that of the parent drug, melphalan, overview
-
-
?
Met-Ala-Ala + H2O
Met + Ala-Ala
-
-
-
?
Met-Ala-Ala + H2O
Met + Ala-Ala
-
-
-
?
Met-Ala-Ala + H2O
Met + Ala-Ala
-
-
-
?
Met-Ala-Ala + H2O
Met + Ala-Ala
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
-
?
Met-Pro + H2O
Met + Pro
-
high activity
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
preferred substrate of wild-type and mutant enzymes
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
best substrate
-
-
?
Met-Pro + H2O
Met + Pro
best substrate
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
-
preferred substrate of isozyme PD II
-
-
?
Met-Pro + H2O
Met + Pro
-
best substrate of isozyme PD II
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro + H2O
Met + Pro
-
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
-
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
-
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
-
-
-
?
Met-Pro-Ala + H2O
Met + Pro-Ala
-
-
-
?
Phe-Pro + H2O
Phe + Pro
-
-
-
-
?
Phe-Pro + H2O
Phe + Pro
-
-
-
-
?
Phe-Pro + H2O
Phe + Pro
-
-
-
-
?
Phe-Pro + H2O
Phe + Pro
-
-
-
?
Phe-Pro + H2O
Phe + Pro
-
-
-
?
Phe-Pro + H2O
Phe + Pro
-
-
-
?
Phe-Pro + H2O
Phe + Pro
-
-
-
?
Phe-Pro + H2O
Phe + Pro
-
-
-
?
Phe-Pro + H2O
Phe + Pro
-
-
-
?
Phe-Pro + H2O
Phe + Pro
-
-
-
?
Phe-Pro + H2O
Phe + Pro
-
-
-
?
Phe-Pro + H2O
Phe + Pro
-
-
-
-
?
Phe-Pro + H2O
Phe + Pro
-
-
-
?
Phe-Pro + H2O
Phe + Pro
-
-
-
?
Phe-Pro-Gly-Pro-Ile + H2O
Phe + Pro-Gly-Pro-Ile
-
-
-
-
?
Phe-Pro-Gly-Pro-Ile + H2O
Phe + Pro-Gly-Pro-Ile
-
-
-
-
?
Phe-Pro-Gly-Pro-Ile + H2O
Phe + Pro-Gly-Pro-Ile
-
-
-
-
?
Pro-Ala + H2O
Pro + Ala
-
-
-
?
Pro-Ala + H2O
Pro + Ala
very low activity
-
-
?
Pro-Ala + H2O
Pro + Ala
very low activity
-
-
?
Pro-Hyp + H2O
Pro + Hyp
-
-
-
-
?
Pro-Hyp + H2O
Pro + Hyp
-
-
-
-
?
Pro-Pro + H2O
Pro + Pro
-
-
-
-
?
Pro-Pro + H2O
Pro + Pro
-
-
-
-
?
Pro-Pro + H2O
Pro + Pro
-
-
-
-
?
Pro-Pro + H2O
Pro + Pro
-
substrate of isozyme PD II, negligible activity with isozyme PD I
-
-
?
Pro-Pro + H2O
Pro + Pro
-
-
-
-
?
Pro-Pro + H2O
Pro + Pro
-
-
-
?
prophalan-D + H2O
?
-
-
-
-
?
prophalan-D + H2O
?
-
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
?
-
-
-
-
?
prophalan-L + H2O
?
-
the L-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
?
-
-
-
-
?
prophalan-L + H2O
?
-
the L-proline prodrug of melphalan
-
-
?
Ser-Pro + H2O
Ser + Pro
-
-
-
-
?
Ser-Pro + H2O
Ser + Pro
-
-
-
-
?
Ser-Pro + H2O
Ser + Pro
-
-
-
?
Ser-Pro + H2O
Ser + Pro
-
-
-
?
Ser-Pro + H2O
Ser + Pro
-
preferred substrate of isozyme PD I
-
-
?
Ser-Pro + H2O
Ser + Pro
-
best substrate of isozyme PD I
-
-
?
Ser-Pro + H2O
Ser + Pro
-
-
-
-
?
Ser-Pro + H2O
Ser + Pro
-
-
-
?
Thr-Pro + H2O
Thr + Pro
-
-
-
-
?
Thr-Pro + H2O
Thr + Pro
-
-
-
-
?
Tyr-Pro + H2O
Tyr + Pro
-
-
-
?
Tyr-Pro + H2O
Tyr + Pro
-
-
-
-
?
Tyr-Pro + H2O
Tyr + Pro
-
-
-
?
Tyr-Pro-Phe-Pro-Gly-Pro-Ile + H2O
Tyr + Pro-Phe-Pro-Gly-Pro-Ile
-
i.e. BCM-7, beta-casomorphin 7
-
-
?
Tyr-Pro-Phe-Pro-Gly-Pro-Ile + H2O
Tyr + Pro-Phe-Pro-Gly-Pro-Ile
-
i.e. BCM-7, beta-casomorphin 7
-
-
?
Tyr-Pro-Phe-Pro-Gly-Pro-Ile + H2O
Tyr + Pro-Phe-Pro-Gly-Pro-Ile
-
i.e. BCM-7, beta-casomorphin 7
-
-
?
Val-Pro + H2O
Val + Pro
-
-
-
-
?
Val-Pro + H2O
Val + Pro
-
-
-
-
?
Val-Pro + H2O
Val + Pro
-
-
-
?
Val-Pro + H2O
Val + Pro
-
-
-
?
Val-Pro + H2O
Val + Pro
-
-
-
?
Val-Pro + H2O
Val + Pro
-
-
-
?
Val-Pro + H2O
Val + Pro
-
-
-
-
?
Val-Pro + H2O
Val + Pro
-
-
-
?
additional information
?
-
-
OPAA-2 can hydrolyze organophosphorus acid nerve agents, such as sarin and soman. OPAA-2 has been reclassified as a prolidase because it can also efficiently hydrolyze X-Pro dipeptides. The enzyme OPAA-2 shows activity with P-F, P-C and P-O bonds. It can also preferentially cleave the dipeptides Leu-Pro and Ala-Pro and is specific for dipeptides with proline in the C-terminal position, but shows no activity with the substrates Pro-Leu and Pro-Gly
-
-
?
additional information
?
-
-
the bifunctional enzyme is active on the nerve agent organophosphate substrate diisopropyl fluorophosphate, DFP, producing N,N'-diisopropyldiamidophosphate, binding structure modelling, overview
-
-
?
additional information
?
-
-
OPAA-2 can hydrolyze organophosphorus acid nerve agents, such as sarin and soman. OPAA-2 has been reclassified as a prolidase because it can also efficiently hydrolyze X-Pro dipeptides. The enzyme OPAA-2 shows activity with P-F, P-C and P-O bonds. It can also preferentially cleave the dipeptides Leu-Pro and Ala-Pro and is specific for dipeptides with proline in the C-terminal position, but shows no activity with the substrates Pro-Leu and Pro-Gly
-
-
?
additional information
?
-
-
the bifunctional enzyme is active on the nerve agent organophosphate substrate diisopropyl fluorophosphate, DFP, producing N,N'-diisopropyldiamidophosphate, binding structure modelling, overview
-
-
?
additional information
?
-
-
the enzyme from guinea pig brain can also cleave substrates without a prolyl residue
-
-
?
additional information
?
-
-
the decreasing order of preference for the P1 residue in the Xaa-Pro dipeptides is Ala, Ser, Phe=Lys, Met, Leu, Gly, Arg, Pro, Val, Tyr, Ile, His, Asp
-
-
?
additional information
?
-
-
enzyme additionally catalyzes the stereoselective hydrolysis of organophosphate triesters and organophosphate diesters such as (S)-methyl phenyl 4-nitrophenyl phosphate with 70fold preferrence for the (S)-enantiomer. Enzyme hydrolyzes 4-nitrophenyl analogs of sarin, soman, and VX
-
-
?
additional information
?
-
-
cleaves imidodipeptides with C-terminal proline or hydroxyproline
-
?
additional information
?
-
-
the acive enzyme form is N-glycosylated, unglycosylated enzyme is not catalytically active
-
?
additional information
?
-
-
the enzyme is involved in collagen metabolism
-
?
additional information
?
-
-
the enzyme is involved in collagen metabolism, enzyme activity is regulated through the beta1 integrin receptor
-
?
additional information
?
-
-
the enzyme plays an important role in recycling of proline for collagen synthesis and cell growth, regulation by phosphorylation and dephosphorylation
-
?
additional information
?
-
-
substrate specificity of wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
enzyme additionally hydrolyzes organophosphorous compounds like soman
-
-
?
additional information
?
-
-
enzyme additionally hydrolyzes organophosphorous compounds such as soman
-
-
?
additional information
?
-
-
alpha-ketoglutarate increases activities of prolidase, which is known to play an important role in collagen metabolism, in fibroblasts, N-benzyloxycarbonyl-L-proline, a prolidase inhibitor, inhibits procollagen synthesis by alpha-ketoglutarate in fibroblasts, alpha-ketoglutarate diminishes UVB-induced wrinkle formation by increasing collagen production, through a pathway that involves prolidase activation, regulation, overview
-
-
?
additional information
?
-
-
interleukin-1beta action and inhibition, resulting in increase in beta1-integrin receptor, NF-kappaB expressions, and increase in phosphorylation of FAK, does deregulate the collagen metabolism, but does not influence the prolidase activity, while metalloproteinase MMP-2 and MMP-9 activities are activated, overview
-
-
?
additional information
?
-
-
prolidase deficiency causes a rare autosomal recessive disease, characterized by a wide range of clinical outcomes, including severe skin lesions, mental retardation, and infections of the respiratory tract
-
-
?
additional information
?
-
-
prolidase is involved in the final stage of degradation in collagen catabolism
-
-
?
additional information
?
-
-
prolidase plays an important role in enhancement of collagen biosynthesis at post-translational level
-
-
?
additional information
?
-
-
prolidase, a specific iminopeptidase involved in collagen turnover, is especially active in growing tissues, the final step of collagen degradation is mediated by prolidase, the cytosolic enzyme specifically splits iminopeptides with C-terminal proline or hydroxyproline, which together contribute 21% of collagen
-
-
?
additional information
?
-
-
the enzyme catalyzes the final step of collagen degradation and plays an important role in collagen biosynthesis
-
-
?
additional information
?
-
-
the enzyme is relevant in the latest stage of protein catabolism, particularly of those molecules rich in imino acids such as collagens, thus being involved in matrix remodelling, overview, prolidase has an antitoxic effect against some organophosphorus molecules, can be used in dietary industry as bitterness reducing agent and is used as target enzyme for specific melanoma prodrug activation, prolidase deficiency is a rare recessive disorder caused by mutations in the prolidase gene and characterized by severe skin lesions, overview
-
-
?
additional information
?
-
-
the enzyme plays an important role in the recycling of proline from imidodipeptides, mostly derived from degradation products of collagen, for resynthesis of collagen and other proline-containing proteins, prolidase-dependent regulation of collagen biosynthesis, pathogenic mechanisms in enzyme deficiency, overview
-
-
?
additional information
?
-
-
prolidase is a Mn2+-dependent exo- or dipeptidase that cleaves imidodipeptides containing C-terminal proline or hydroxyproline, substrate specificity of native and recombinant enzymes, molecular modeling, overview
-
-
?
additional information
?
-
-
prolidase is an unusual metalloenzyme that cleaves the iminodipeptides containing a proline or hydroxyproline residue at the C-terminal end, it is a dipeptidase able to hydrolyse the peptide bond in dipeptides containing respectively a N- or C-terminal proline or hydroxyproline residue, overview, recombinant human prolidase expressed in Pichia pastoris catalyzes the hydrolysis of organophosphorus compounds as well as the digestion of Gly-Pro dipeptides
-
-
?
additional information
?
-
-
specific activities with melphalan and prodrugs in cancer cell lines, overview
-
-
?
additional information
?
-
-
substrate specificity, prolidase is a cytosolic imidodipeptidase, which specifically splits imidodipeptides with C-terminal proline or hydroxyproline, overview
-
-
?
additional information
?
-
-
prolidases are specific for dipeptides with proline in the trans configuration in the P1' position and nonpolar residues in the P1 position
-
-
?
additional information
?
-
human prolidase is the only metalloenzyme among the peptidases that cleaves the iminodipeptides containing a proline or hydroxyproline residue at the C-terminal end
-
-
?
additional information
?
-
-
human prolidase is the only metalloenzyme among the peptidases that cleaves the iminodipeptides containing a proline or hydroxyproline residue at the C-terminal end
-
-
?
additional information
?
-
-
prolidase hydrolyses dipeptides containing proline or hydroxyproline as the C-terminal amino acid
-
-
?
additional information
?
-
-
prolidase is a exopeptidase that cleaves iminodipeptides containing C-terminal proline or hydroxyproline
-
-
?
additional information
?
-
-
prolidase is a manganese-requiring homodimeric iminodipeptidase, which releases carboxy-terminal proline or hydroxyproline from oligopeptides
-
-
?
additional information
?
-
-
prolidase is an exopeptidase
-
-
?
additional information
?
-
-
prolidase is an exopeptidase
-
-
?
additional information
?
-
-
prolidase is an exopeptidase cleaving C-terminally proline and hydroxyproline from iminodipeptides
-
-
?
additional information
?
-
-
prolidase is an iminodipeptidase, which releases C-terminal proline or hydroxyproline from oligopeptides
-
-
?
additional information
?
-
-
the enzyme is also active with diisopropyl phosphorofluoridate, an organophosphorus nerve reagent
-
-
?
additional information
?
-
-
no substrate: Pro-Pro, Gly-Pro
-
-
?
additional information
?
-
-
the enzyme from Lactococcus casei can also cleave substrates without a prolyl residue
-
-
?
additional information
?
-
-
the enzyme from Lactococcus casei can also cleave substrates without a prolyl residue
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
no substrate: Pro-Pro, Gly-Pro
-
-
?
additional information
?
-
-
the enzyme only hydrolyzes dipeptides with a proline in the C-terminus and cannot cleave dipeptides with proline in the N-terminus
-
-
?
additional information
?
-
-
the enzyme is likely a serine proteinase
-
-
?
additional information
?
-
-
the enzyme is likely a serine proteinase
-
-
?
additional information
?
-
-
the enzyme is likely a serine proteinase
-
-
?
additional information
?
-
substrate specificity, dependent on the catalytic metal cation, overview, no activity with Pro-Pro, Glu-Pro, Gly-Pro, Asp-Pro, Leu-Leu-Pro, and Leu-Val-Pro, molecular modeling, overview
-
-
?
additional information
?
-
-
does not degrade L-Glu-L-Pro, Gly-L-Pro, L-Pro-L-Pro, L-Leu-L-Leu-L-Pro, L-Leu-L-Val-L-Pro, and L-Asp-L-Pro
-
-
?
additional information
?
-
-
wild-type Lactococcus lactis prolidase preferably hydrolyzes Xaa-Pro dipeptides where Xaa is a hydrophobic amino acid. Anionic Glu-Pro and Asp-Pro dipeptides cannot be hydrolyzed at any observable rates, and the hydrolysis of cationic Arg-Pro and Lys-Pro dipeptides is at about one tenth of the rate of Leu-Pro, no activity with tripeptides Leu-Leu-Pro and Leu-Val-Pro, substrate specificity of wild-type and mutant enzymes, the enzyme activity depends highly on the metal ion, overview
-
-
?
additional information
?
-
substrate specificity, dependent on the catalytic metal cation, overview, no activity with Pro-Pro, Glu-Pro, Gly-Pro, Asp-Pro, Leu-Leu-Pro, and Leu-Val-Pro, molecular modeling, overview
-
-
?
additional information
?
-
-
substrate specificity, dependent on the catalytic metal cation, overview, no activity with Pro-Pro, Glu-Pro, Gly-Pro, Asp-Pro, Leu-Leu-Pro, and Leu-Val-Pro, molecular modeling, overview
-
-
?
additional information
?
-
decreasing order of preference for the N-terminal residue of the Xaa-Pro dipeptides in presence of Mn2+ ions is Leu, Pro, Phe, Met, Arg, Lys, Ile, Ser, His, Ala, Gly, Val, Asp while in that of Zn2+ ions is Leu, Phe, Met, Pro, Arg, Lys, Ala, Ile, Ser, Gly, Val, Asp
-
-
?
additional information
?
-
-
decreasing order of preference for the N-terminal residue of the Xaa-Pro dipeptides in presence of Mn2+ ions is Leu, Pro, Phe, Met, Arg, Lys, Ile, Ser, His, Ala, Gly, Val, Asp while in that of Zn2+ ions is Leu, Phe, Met, Pro, Arg, Lys, Ala, Ile, Ser, Gly, Val, Asp
-
-
?
additional information
?
-
decreasing order of preference for the N-terminal residue of the Xaa-Pro dipeptides in presence of Mn2+ ions is Leu, Pro, Phe, Met, Arg, Lys, Ile, Ser, His, Ala, Gly, Val, Asp while in that of Zn2+ ions is Leu, Phe, Met, Pro, Arg, Lys, Ala, Ile, Ser, Gly, Val, Asp
-
-
?
additional information
?
-
-
PepQ is a cytoplasmic prolidase that specifically liberated proline from dipeptides with increased activity under high salt conditions, PepX, a X-prolyl-dipeptidyl aminopeptidase, and PepI, a iminopeptidase, are unaffected, overview
-
-
?
additional information
?
-
-
prolidases are specific for dipeptides with proline in the trans configuration in the P1' position and nonpolar residues in the P1 position
-
-
?
additional information
?
-
-
Pfprol has a narrow substrate specificity, only hydrolyzing dipeptides with a proline in the C-terminus and nonpolar amino acids, Leu, Met, Val, Phe, or Ala, in the N-terminal position. Pfprol cannot cleave dipeptides with proline in the N-terminus. Substrate binding, structure-function relationship, overview. No activity on organophosphorus nerve agents sarin, cyclosarin, and soman, but with diisopropyl phosphorofluoridate
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
-
substrate specificity of isozymes, overview
-
-
?
additional information
?
-
-
lack of prolidase I leads to prolidase deficiency, a disease characterized by intractable skin lesions, recurrent respiratory infections, and mental retardation, physiologic roles of prolidase isoenzymes, PD I functions by way of an intestinal peptide carrier, which may be regulated by the uptake of various iminodipeptides, intestinal PD II also participates in absorption of proline and other amino acids early in life, overview
-
-
?
additional information
?
-
-
guinea pig brain: general dipeptidase and prolinase activity
-
-
?
additional information
?
-
-
enzyme also acts on hydroxyproline dipeptides and amides
-
-
?
additional information
?
-
-
no or poor activity with prophalan-D and melphalan
-
-
?
additional information
?
-
-
prolidase plays an important role in collagen biosynthesis
-
-
?
additional information
?
-
enzyme exhibits allosteric behavior and substrate inhibition toward dipeptides Leu-Pro, Pro-Pro, His-Pro, Lys-Pro and Tyr-Pro. The order of preference for the N-terminal residue of the Xaa-Pro dipeptides is similar in presence of Mn2+ ions (in decreasing order: Phe, Ser, Met, Leu, Ala, Pro, His, Arg, Ile, Gly, Val, Asp) and Zn2+ ions (0.005 mM) (Met, Phe, SerN, Leu, Ala, Pro, Arg, Lys, Ile=Gly, Val, Asp). The activity towards all the substrates is 4-5 times higher in presence of Mn2+ than Zn2+ ions
-
-
?
additional information
?
-
Xaa-Pro dipeptidase (XPD) specifically cleaves a trans Xaa-Pro peptide bond in dipeptides with a prolyl residue at the carboxy-terminus
-
-
?
additional information
?
-
Xaa-Pro dipeptidase (XPD) specifically cleaves a trans Xaa-Pro peptide bond in dipeptides with a prolyl residue at the carboxy-terminus
-
-
?
additional information
?
-
Xaa-Pro dipeptidase (XPD) specifically cleaves a trans Xaa-Pro peptide bond in dipeptides with a prolyl residue at the carboxy-terminus
-
-
?
additional information
?
-
enzyme exhibits allosteric behavior and substrate inhibition toward dipeptides Leu-Pro, Pro-Pro, His-Pro, Lys-Pro and Tyr-Pro. The order of preference for the N-terminal residue of the Xaa-Pro dipeptides is similar in presence of Mn2+ ions (in decreasing order: Phe, Ser, Met, Leu, Ala, Pro, His, Arg, Ile, Gly, Val, Asp) and Zn2+ ions (0.005 mM) (Met, Phe, SerN, Leu, Ala, Pro, Arg, Lys, Ile=Gly, Val, Asp). The activity towards all the substrates is 4-5 times higher in presence of Mn2+ than Zn2+ ions
-
-
?
additional information
?
-
Xaa-Pro dipeptidase (XPD) specifically cleaves a trans Xaa-Pro peptide bond in dipeptides with a prolyl residue at the carboxy-terminus
-
-
?
additional information
?
-
Xaa-Pro dipeptidase (XPD) specifically cleaves a trans Xaa-Pro peptide bond in dipeptides with a prolyl residue at the carboxy-terminus
-
-
?
additional information
?
-
Xaa-Pro dipeptidase (XPD) specifically cleaves a trans Xaa-Pro peptide bond in dipeptides with a prolyl residue at the carboxy-terminus
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Gly-Pro + H2O
Glycine + proline
-
-
-
?
melphalan + H2O
?
-
prolidase-dependence of prodrug cytotoxicity in the cell lines compared to that of the parent drug, melphalan, overview
-
-
?
prophalan-D + H2O
?
-
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
-
-
?
additional information
?
-
prophalan-L + H2O
?
-
the L-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
?
-
the L-proline prodrug of melphalan
-
-
?
additional information
?
-
-
the enzyme is involved in collagen metabolism
-
?
additional information
?
-
-
the enzyme is involved in collagen metabolism, enzyme activity is regulated through the beta1 integrin receptor
-
?
additional information
?
-
-
the enzyme plays an important role in recycling of proline for collagen synthesis and cell growth, regulation by phosphorylation and dephosphorylation
-
?
additional information
?
-
-
alpha-ketoglutarate increases activities of prolidase, which is known to play an important role in collagen metabolism, in fibroblasts, N-benzyloxycarbonyl-L-proline, a prolidase inhibitor, inhibits procollagen synthesis by alpha-ketoglutarate in fibroblasts, alpha-ketoglutarate diminishes UVB-induced wrinkle formation by increasing collagen production, through a pathway that involves prolidase activation, regulation, overview
-
-
?
additional information
?
-
-
interleukin-1beta action and inhibition, resulting in increase in beta1-integrin receptor, NF-kappaB expressions, and increase in phosphorylation of FAK, does deregulate the collagen metabolism, but does not influence the prolidase activity, while metalloproteinase MMP-2 and MMP-9 activities are activated, overview
-
-
?
additional information
?
-
-
prolidase deficiency causes a rare autosomal recessive disease, characterized by a wide range of clinical outcomes, including severe skin lesions, mental retardation, and infections of the respiratory tract
-
-
?
additional information
?
-
-
prolidase is involved in the final stage of degradation in collagen catabolism
-
-
?
additional information
?
-
-
prolidase plays an important role in enhancement of collagen biosynthesis at post-translational level
-
-
?
additional information
?
-
-
prolidase, a specific iminopeptidase involved in collagen turnover, is especially active in growing tissues, the final step of collagen degradation is mediated by prolidase, the cytosolic enzyme specifically splits iminopeptides with C-terminal proline or hydroxyproline, which together contribute 21% of collagen
-
-
?
additional information
?
-
-
the enzyme catalyzes the final step of collagen degradation and plays an important role in collagen biosynthesis
-
-
?
additional information
?
-
-
the enzyme is relevant in the latest stage of protein catabolism, particularly of those molecules rich in imino acids such as collagens, thus being involved in matrix remodelling, overview, prolidase has an antitoxic effect against some organophosphorus molecules, can be used in dietary industry as bitterness reducing agent and is used as target enzyme for specific melanoma prodrug activation, prolidase deficiency is a rare recessive disorder caused by mutations in the prolidase gene and characterized by severe skin lesions, overview
-
-
?
additional information
?
-
-
the enzyme plays an important role in the recycling of proline from imidodipeptides, mostly derived from degradation products of collagen, for resynthesis of collagen and other proline-containing proteins, prolidase-dependent regulation of collagen biosynthesis, pathogenic mechanisms in enzyme deficiency, overview
-
-
?
additional information
?
-
-
prolidases are specific for dipeptides with proline in the trans configuration in the P1' position and nonpolar residues in the P1 position
-
-
?
additional information
?
-
-
PepQ is a cytoplasmic prolidase that specifically liberated proline from dipeptides with increased activity under high salt conditions, PepX, a X-prolyl-dipeptidyl aminopeptidase, and PepI, a iminopeptidase, are unaffected, overview
-
-
?
additional information
?
-
-
prolidases are specific for dipeptides with proline in the trans configuration in the P1' position and nonpolar residues in the P1 position
-
-
?
additional information
?
-
-
lack of prolidase I leads to prolidase deficiency, a disease characterized by intractable skin lesions, recurrent respiratory infections, and mental retardation, physiologic roles of prolidase isoenzymes, PD I functions by way of an intestinal peptide carrier, which may be regulated by the uptake of various iminodipeptides, intestinal PD II also participates in absorption of proline and other amino acids early in life, overview
-
-
?
additional information
?
-
-
prolidase plays an important role in collagen biosynthesis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cobalt
-
2 atoms per subunit are required for optimum activity
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
Ca2+
-
can substitute for Mn2+ by less than 30%
Co2+
-
activates
Co2+
-
can substitute for Mn2+ by less than 30%
Co2+
-
activates, preferred metal ion
Co2+
-
requires Co2+ in addition to one cobalt atom bound per subunit
Co2+
dinuclear metal cluster in the active site, binding of 2 Co2+ per subunit
Co2+
-
one Co-bound dinuclear metal cluster per monomer, Co1 is the tight binding, Co2 the loose binding metal center. Wild-type exhibits maximal activity in presence of 0.5 mM Co2+, less than 20% residual activity with 10 mM Co2+
Co2+
-
metalloenzyme, required for activity, a homodimer having one Co-bound dinuclear metal cluster per monomer with one tightly bound Co1 and one loosely bound Co2 cobalt site, 5 amino acids that function as metal-binding residues: His284 and Glu313 solely bind to the first cobalt centre, Co1, Asp209 to the second cobalt centre, Co2, and Asp220 and Glu327 to both Co2+ ions
Co2+
-
highly activating, one Co2+ per enzyme subunit
Fe2+
-
best activating divalent ion
Mg2+
-
can substitute for Mn2+ by less than 30%
Mn2+
-
requires divalent cations for activity, most active with manganese
Mn2+
-
the enzyme harbors binuclear Mn2+ ions within the active site
Mn2+
-
stabilization of enzyme against inhibition by Ni2+
Mn2+
-
presence of 1 mM in the assay
Mn2+
-
required for activity
Mn2+
-
dependent on, metallopeptidase, complex formation with anthracyclines
Mn2+
-
required for enzyme activation
Mn2+
-
dependent on, best divalent cation
Mn2+
-
metalloenzyme, required for activity, each subunit contains two ions Mn2+, binding structure, overview
Mn2+
-
metalloenzyme, required for activity, the active site Mn2+ cation is simultaneously ligated to the prolyl carboxyl group and the amido oxygen of the preceding residue of the trans X-Pro dipeptides
Mn2+
-
required, plays an important role in the activation and functional regulation of the enzyme
Mn2+
-
40 mM, dependent on
Mn2+
-
activation of prolidase requires preincubation with 2 mM Mn2+
Mn2+
-
requires divalent cations for activity, most active with manganese
Mn2+
the protein can host two metal ions in the active site of each constituent monomer, two different kinds of metals, Mn and Zn can be simultaneously present in the protein active sites with the protein partially maintaining its enzymatic activity. Dimeric metalloenzyme, one of the two active sites is occupied by two Zn ions and the second one by one Zn and one Mn ion, in both dinuclear units a histidine residue is bound to a Zn ion, binding structure, overview
Mn2+
-
requires divalent cations for activity, most active with manganese
Mn2+
two preferred metal cations: zinc and manganese, the substrate Leu-Pro is preferred with zinc, whereas Arg-Pro is preferred with manganese
Mn2+
maximum activity in presence of Mn2+ ions, addition of 1 mM to the assay
Mn2+
-
Co2+ can be replaced by Mn2+
Mn2+
-
requires divalent cations for activity, most active with manganese
Mn2+
-
activation of prolidase requires preincubation with 2 mM Mn2+
Mn2+
maximum activity in presence of Mn2+ ions, addition of 1 mM to the assay
Zn2+
-
can substitute for Mn2+ by less than 30%
Zn2+
the protein can host two metal ions in the active site of each constituent monomer, two different kinds of metals, Mn and Zn can be simultaneously present in the protein active sites with the protein partially maintaining its enzymatic activity. Dimeric metalloenzyme, one of the two active sites is occupied by two Zn ions and the second one by one Zn and one Mn ion, in both dinuclear units a histidine residue is bound to a Zn ion, binding structure, overview
Zn2+
-
requires divalent cations for activity, most active with zinc
Zn2+
-
required for optimum activity
Zn2+
two preferred metal cations: zinc and manganese, the substrate Leu-Pro is preferred with zinc, whereas Arg-Pro is preferred with manganese
Zn2+
2 Zn2+ bound to the subunit in the crystallized enzyme only replacing the Co2+ ions, binding structure via 5 coordinates
Zn2+
-
interaction with amino acid residues D209, D220, H284, E313 and E327, overview
additional information
-
OPAA-2 has a conserved binuclear metal center
additional information
determination of enzyme samples metal contents, overview
additional information
-
determination of enzyme samples metal contents, overview
additional information
-
no significant effect by Ca2+ at 1 mM
additional information
the substrate specificity is dependent on the catalytic metal cation, molecular modeling, overview
additional information
-
the enzyme requires divalent cations for activity
additional information
-
PepQ shows increased activity under high salt conditions
additional information
-
the enzyme contains a dinuclear metal center bridged by a water molecule or hydroxide ion. The metal cluster is essential for the activation of catalysis. It functions to activate a nucleophile for the reaction, as well as participating in substrate binding and stabilizing the transition state. The dipeptidase is maximally active with the addition of the divalent cations Co2+ and Mn2+ and it cannot be substituted with other divalent cations, i.e Mg2+, Ca2+, Fe2+, Ni2+, Cu2+, or Zn2+, under aerobic conditions
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2S,3R)-3-amino-2-hydroxy-5-methyl-hexanoyl-proline
-
(2S,3R)-3-amino-2-hydroxy-5-methylhexanoyl-proline
-
1,2-Cylcopentanedicarboxylic acid
-
-
acetic acid
-
inhibits 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
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
diisopropylfluorophosphate
-
87% inhibition at 1 mM
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
-
His-Pro
substrate inhibition
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-valine
-
inhibitory to enzyme isoform prolidase I, activating isoform prolidase II
L-valinyl-D-boroproline
-
-
Leu-Pro
substrate inhibition
Lys-Pro
substrate inhibition
melanin
-
30% inhibition at 0.1 mg/ml, reverses inhibition of prolidase by netilmicin
N,N'-diisopropyldiamidofluorophosphate
-
i.e. DDFP or mipafox
N-Benzyloxycarbonyl-L-proline
N-[N'-(2-bromoethyl)-N'-nitrosocarbamoyl]-L-proline
-
-
netilmicin
-
80% inhibition at 0.01 mM, reversible by melanin
paracetamol
-
mechanism of PLD inhibition by paracetamol is noncompetitive inhibition
phenylacetyl-thioproline
-
-
Phenylmethylsulfonylfluoride
-
88.5% inhibition at 1 mM
Phosphonocarboxylates
-
-
-
Pro-Pro
substrate inhibition
trans-1,2-cyclopentanedicarboxylate
-
-
Tyr-Pro
substrate inhibition
Z-Pro
-
roughly 80% inhibition at 2.53 mM
1,10-phenanthroline
-
-
2-mercaptoethanol
-
1 mM, 55% residual activity
2-mercaptoethanol
-
weakly
Ag+
-
-
Cd2+
-
-
Co2+
-
slight inhibition at 0.1-1.0 mM
Cu2+
-
-
Cu2+
-
85% inhibition at 1 mM
dithiothreitol
-
-
EDTA
-
-
EDTA
-
1 mM, 70% residual activity
Hg2+
-
-
Hg2+
-
98% inhibition at 1 mM
iodoacetate
-
-
Mg2+
-
-
Mg2+
-
slight inhibition at 0.1-1.0 mM
N-Benzyloxycarbonyl-L-proline
-
90% inhibition after incubation of cell extracts at a 1:1 ratio of inhibitor to substrate Gly-L-Pro. Long-term incubation of fibroblasts with inhibitor causes mitochondria depolarization and increased cellular death
N-Benzyloxycarbonyl-L-proline
-
50% inhibition at 5 mM
N-Benzyloxycarbonyl-L-proline
-
-
N-Benzyloxycarbonyl-L-proline
-
competitive, 60-83% inhibition levels of the enzyme from different cancer cell lines, overview
N-Benzyloxycarbonyl-L-proline
-
daily injection of inhibitor for 3 weeks results in significant reduction of enzyme activity in erythrocyte. Inhibitor is not degraded in vivo
N-Benzyloxycarbonyl-L-proline
-
inhibits isozyme PD I dose-dependently, but shows no inhibition of isozyme PD II at up to 1 mM
N-Benzyloxycarbonyl-L-proline
-
inhibits PD I, but not PD II
N-Benzyloxycarbonyl-L-proline
-
-
N-Benzyloxycarbonyl-L-proline
-
competitive
Ni2+
-
-
Ni2+
-
Ni2+ (0.05 and 0.15mM) is a competitive inhibitor of prolidase with respect to Mn2+
NiCl2
-
specific inhibition of enzyme activity in situ. Increasing concentration of Mn2+ stabilizes against Ni2+ inhibition
NiCl2
-
inhibits isozye PD II much more effectively than isozyme PD I
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
Zn2+
-
slightly
Zn2+
-
56% inhibition at 1 mM
Zn2+
inhibitory above 0.01 mM
additional information
-
effects of sulfated amino acids on enzyme-deficient erythrocytes, overview
-
additional information
-
carmustine does not inhibit MCF-7 cells prolidase activity
-
additional information
-
no significant effect by 2-mercaptoethanol at 1 mM
-
additional information
-
insensitive to EDTA
-
additional information
-
mechanism of inhibition
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(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
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-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-serine
-
activation of isoforms prolidase I and prolidase II
D-valine
-
activation of isoforms prolidase I and prolidase II
diethyldithiocarbamate
-
activation
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-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
-
D,L-homocysteine
-
enhances the activity of isozyme prolidase I at low concentration
D,L-homocysteine
-
weakly enhances the activity of isozyme prolidase II
D,L-methionine
-
slightly enhances the activity of isozyme prolidase I at low concentration
D,L-methionine
-
the activity of isozyme prolidase II against L-Met-L-Pro is enhanced by D,L-methionine
D-methionine
-
the activity of isozyme prolidase I against Gly-L-Pro is strongly enhanced by D-methionine
D-methionine
-
the activity of isozyme prolidase II against L-Met-L-Pro is enhanced by D-methionine
EDTA
-
slight activation at 1.0 mM
glycine
-
activation of activity against substrates L-Pro-L-Ala, L-Pro-L-Val, L-Pro-L-Met, and L-Pro-L-Asp
glycine
-
activation of isoforms prolidase I and prolidase II
L-methionine
-
slightly enhances the activity of isozyme prolidase I at low concentration
L-methionine
-
the activity of isozyme prolidase II against L-Met-L-Pro is enhanced by L-methionine
NO
-
NO stimulate both prolidase activity and collagen biosynthesis in fibroblasts, increase in the enzyme activity is due to increase in the enzyme phosphorylation on serine/threonine residue
NO
-
NO-donors such as SIN I and DETA/NO increase enzyme activity in time- and dose-dependent manner. Enzyme activity also increases upon transfection of cells with iNOS. Increased enzymic activity is accompanied by increase in serine/threonine phosphorylation of enzyme
additional information
-
phosphorylation at four S109, S134, S198, S236, one T86, and two Y117, Y124 putative sites for phosphorylation, mediated respectively by Mapk pathway and NO/cGMP signaling, upregulate prolidase activity
-
additional information
-
prolidase activity is dependent on the interaction of collagen with the beta1-integrin receptor subunit
-
additional information
-
N-acetyl-L-methionine has no effect on activity of isozymes prolidase I and prolidase II
-
additional information
-
increased enzyme activity in patients with casculogenic erectile dysfunction, highest enzyme activity in patients with arterial insufficiency
-
additional information
-
no significant effect by 2-mercaptoethanol at 1 mM
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.91
Met-Ala-Ala
pH 7.0, 97°C, recombinant wild-type
1.8
Met-Pro-Ala
pH 7.0, 97°C, recombinant wild-type
additional information
additional information
-
0.127
Ala-Pro
-
pH 7.8, 37°C, recombinant His-tagged wild-type enzyme
1.495
Ala-Pro
-
pH 7.8, 37°C, recombinant His-tagged mutant F822A
2.219
Ala-Pro
-
pH 7.8, 37°C, recombinant His-tagged mutant V833A
2.397
Ala-Pro
-
pH 7.8, 37°C, recombinant His-tagged mutant Y844A
2.72
Ala-Pro
-
pH 7.8, 37°C, recombinant His-tagged mutant H859A
8.3
Ala-Pro
-
native prolidase
0.006
Gly-L-Pro
-
-
1.64
Gly-L-Pro
-
pH 7.8, 37°C, presence of 20 mM glycine, prolidase I
2.13
Gly-L-Pro
-
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
2.3
Gly-L-Pro
-
pH 7.8, 37°C, presence of 20 mM D-valine, prolidase I
2.59
Gly-L-Pro
-
pH 7.8, 37°C, prolidase I
2.63
Gly-L-Pro
-
pH 7.8, 37°C, presence of 20 mM L-valine, prolidase I
6.23
Gly-L-Pro
-
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
0.14
Gly-Pro
-
-
2.88 - 2.9
Gly-Pro
-
prolidase I from normal human and mother of patient with prolidase deficiency
0.39
His-Pro
-
-
0.395
L-Leu-L-Pro
-
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
-
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
-
mutant enzyme S307G, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C
8
L-Leu-L-Pro
-
wild type enzyme, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C
10.1
L-Leu-L-Pro
-
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
-
mutant enzyme S307R, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C
18
L-Leu-L-Pro
-
mutant enzyme S307D, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C
23.3
L-Leu-L-Pro
-
mutant enzyme R293S, in 20 mM sodium citrate (pH 6.5), and 1 mM ZnCl2, at 50°C
0.81
L-Met-L-Pro
-
-
4.11
L-Met-L-Pro
-
pH 7.8, 37°C, presence of 20 mM glycine, prolidase I
4.43
L-Met-L-Pro
-
pH 7.8, 37°C, presence of 20 mM glycine, enzyme from patient with enzyme deficiency
4.65
L-Met-L-Pro
-
pH 7.8, 37°C, presence of 20 mM D-valine, prolidase I
5.39
L-Met-L-Pro
-
pH 7.8, 37°C, presence of 20 mM glycine, prolidase II
5.48
L-Met-L-Pro
-
pH 7.8, 37°C, presence of 20 mM L-valine, enzyme from patient with enzyme deficiency
5.65
L-Met-L-Pro
-
pH 7.8, 37°C, presence of 20 mM L-valine, prolidase II
6.16
L-Met-L-Pro
-
pH 7.8, 37°C, presence of 20 mM D-valine, enzyme from patient with enzyme deficiency
6.33
L-Met-L-Pro
-
pH 7.8, 37°C, presence of 20 mM D-valine, prolidase II
8.83
L-Met-L-Pro
-
pH 7.8, 37°C, presence of 20 mM L-valine, prolidase I
9.2
L-Met-L-Pro
-
pH 7.8, 37°C, prolidase I
9.65
L-Met-L-Pro
-
pH 7.8, 37°C, prolidase II
9.89
L-Met-L-Pro
-
pH 7.8, 37°C, enzyme from patient with enzyme deficiency
6.8
L-Pro-Gly
-
pH 7.8, 37°C, presence of 0.1 mM MnCl2 plus 20 mM glycine
8.6
L-Pro-Gly
-
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
-
pH 7.8, 37°C, presence of 0.1 mM MnCl2, enzyme from patient with enzyme deficiency
13.8
L-Pro-Gly
-
pH 7.8, 37°C, presence of 0.1 mM MnCl2
15.1
L-Pro-Gly
-
pH 7.8, 37°C, presence of 20 mM glycine
16.7
L-Pro-Gly
-
pH 7.8, 37°C, presence of 20 mM glycine, enzyme from patient with enzyme deficiency
18.2
L-Pro-Gly
-
pH 7.8, 37°C, enzyme from patient with enzyme deficiency
26.9
L-Pro-Gly
-
pH 7.8, 37°C
4.2
L-Pro-L-Met
-
pH 7.8, 37°C, presence of 20 mM glycine, enzyme from patient with enzyme deficiency
5
L-Pro-L-Met
-
pH 7.8, 37°C, presence of 0.1 mM MnCl2 plus 20 mM glycine, enzyme from patient with enzyme deficiency
8.1
L-Pro-L-Met
-
pH 7.8, 37°C, enzyme from patient with enzyme deficiency
8.35
L-Pro-L-Met
-
pH 7.8, 37°C, presence of 20 mM glycine
9.7
L-Pro-L-Met
-
pH 7.8, 37°C, presence of 0.1 mM MnCl2, enzyme from patient with enzyme deficiency
9.9
L-Pro-L-Met
-
pH 7.8, 37°C, presence of 0.1 mM MnCl2 plus 20 mM glycine
17.6
L-Pro-L-Met
-
pH 7.8, 37°C
19.1
L-Pro-L-Met
-
pH 7.8, 37°C, presence of 0.1 mM MnCl2
3.2
L-Pro-L-Val
-
pH 7.8, 37°C, presence of 20 mM glycine, enzyme from patient with enzyme deficiency
5.5
L-Pro-L-Val
-
pH 7.8, 37°C, presence of 0.1 mM MnCl2 plus 20 mM glycine, enzyme from patient with enzyme deficiency
7.9
L-Pro-L-Val
-
pH 7.8, 37°C, enzyme from patient with enzyme deficiency
10.1
L-Pro-L-Val
-
pH 7.8, 37°C, presence of 0.1 mM MnCl2, enzyme from patient with enzyme deficiency
14.7
L-Pro-L-Val
-
pH 7.8, 37°C, presence of 20 mM glycine
17.3
L-Pro-L-Val
-
pH 7.8, 37°C, presence of 0.1 mM MnCl2 plus 20 mM glycine
26
L-Pro-L-Val
-
pH 7.8, 37°C
28.6
L-Pro-L-Val
-
pH 7.8, 37°C, presence of 0.1 mM MnCl2
0.06
L-Val-L-Pro
-
-
0.243
L-Val-L-Pro
-
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
-
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
0.2
Leu-Pro
-
-
0.81
Leu-Pro
pH 7.0, 70°C, mutant enzyme A195T/G306S
0.92
Leu-Pro
pH 7.0, 70°C, wild-type enzyme
0.98
Leu-Pro
pH 7.0, 70°C, mutant enzyme E127G/E252D
1.6
Leu-Pro
pH 7.0, 70°C, mutant enzyme E36V
2.92
Leu-Pro
pH 7.0, 70°C, mutant enzyme Y301C/K342N
3
Leu-Pro
-
native prolidase
10.4
Leu-Pro
-
human fibroplasts with prolidase deficiency
1.5
Lys-Pro
-
pH 8.0, 55°C
0.81
Met-Pro
-
-
1.7
Met-Pro
-
pH 8.0, 55°C
1.9
Met-Pro
pH 7.0, 100°C
2.8
Met-Pro
-
native prolidase
3.3
Met-Pro
-
recombinant prolidase
3.4
Met-Pro
pH 7.0, 100°C
5.7
Met-Pro
pH 7.0, 70°C, recombinant wild-type enzyme
5.7
Met-Pro
pH 7.0, 70°C, wild-type enzyme
6.4
Met-Pro
pH 7.0, 35°C, wild-type enzyme
6.4
Met-Pro
pH 7.0, 35°C, recombinant wild-type enzyme
6.8
Met-Pro
pH 7.0, 70°C, recombinant mutant G39E
6.8
Met-Pro
pH 7.0, 70°C, wild-type enzyme G39E
7.5
Met-Pro
pH 7.0, 70°C, recombinant mutant R19G/G39E/K71E/S229T
7.5
Met-Pro
pH 7.0, 70°C, mutant enzyme R19G/G39E/K71E/S229T
7.9
Met-Pro
pH 7.0, 35°C, recombinant mutant R19G/G39E/K71E/S229T
7.9
Met-Pro
pH 7.0, 35°C, mutant enzyme R19G/G39E/K71E/S229T
7.95
Met-Pro
pH 7.0, 100°C, recombinant wild-type enzyme
7.95
Met-Pro
pH 7.0, 100°C, wild-type enzyme
9.2
Met-Pro
pH 7.0, 70°C, recombinant mutant R19G/K71E/S229T
9.2
Met-Pro
pH 7.0, 70°C, mutant enzyme R19G/K71E/S229T
9.8
Met-Pro
pH 7.0, 97°C, recombinant wild-type
11.1
Met-Pro
pH 7.0, 100°C, recombinant mutant R19G/G39E/K71E/S229T
11.1
Met-Pro
pH 7.0, 100°C, mutant enzyme R19G/G39E/K71E/S229T
11.3
Met-Pro
pH 7.0, 35°C, recombinant mutant R19G/K71E/S229T
11.3
Met-Pro
pH 7.0, 35°C, mutant enzyme R19G/K71E/S229T
13
Met-Pro
pH 7.0, 35°C, recombinant mutant G39E
13
Met-Pro
pH 7.0, 35°C, mutant enzyme G39E
13.7
Met-Pro
pH 7.0, 100°C, recombinant mutant R19G/K71E/S229T
13.7
Met-Pro
pH 7.0, 100°C, mutant enzyme R19G/K71E/S229T
14.5
Met-Pro
pH 7.0, 100°C, recombinant mutant G39E
14.5
Met-Pro
pH 7.0, 100°C, wild-type enzyme G39E
0.76
Phe-Pro
-
-
1.3
Phe-Pro
-
pH 8.0, 55°C
20
Phe-Pro
-
native prolidase
0.38
Pro-Pro
-
-
0.41
Val-Pro
-
-
4.2
Val-Pro
-
native prolidase
additional information
additional information
-
-
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes
-
additional information
additional information
-
kinetics and substrate specificity of wild-type and mutant enzymes, overview
-
additional information
additional information
the recombinant enzyme shows an allosteric behaviour, overview
-
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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
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evolution
XPD belongs to the M24B family of metalloenzymes. Xanthomonas spp. possess two different isoforms of XPD (48 and 43 kDa) which share about 24% sequence identity. The XPD of 43 kDa in size (XPD43) from Xanthomonas spp. is unusual as it lacks the strictly conserved tyrosine residue (equivalent to Tyr387 in Escherichia coli aminopeptidase P). XPD is ubiquitous in nature and has been isolated from mammals, bacteria, and archaea
evolution
-
XPD belongs to the M24B family of metalloenzymes. Xanthomonas spp. possess two different isoforms of XPD (48 and 43 kDa) which share about 24% sequence identity. The XPD of 43 kDa in size (XPD43) from Xanthomonas spp. is unusual as it lacks the strictly conserved tyrosine residue (equivalent to Tyr387 in Escherichia coli aminopeptidase P). XPD is ubiquitous in nature and has been isolated from mammals, bacteria, and archaea
-
evolution
-
XPD belongs to the M24B family of metalloenzymes. Xanthomonas spp. possess two different isoforms of XPD (48 and 43 kDa) which share about 24% sequence identity. The XPD of 43 kDa in size (XPD43) from Xanthomonas spp. is unusual as it lacks the strictly conserved tyrosine residue (equivalent to Tyr387 in Escherichia coli aminopeptidase P). XPD is ubiquitous in nature and has been isolated from mammals, bacteria, and archaea
-
evolution
-
XPD belongs to the M24B family of metalloenzymes. Xanthomonas spp. possess two different isoforms of XPD (48 and 43 kDa) which share about 24% sequence identity. The XPD of 43 kDa in size (XPD43) from Xanthomonas spp. is unusual as it lacks the strictly conserved tyrosine residue (equivalent to Tyr387 in Escherichia coli aminopeptidase P). XPD is ubiquitous in nature and has been isolated from mammals, bacteria, and archaea
-
evolution
-
XPD belongs to the M24B family of metalloenzymes. Xanthomonas spp. possess two different isoforms of XPD (48 and 43 kDa) which share about 24% sequence identity. The XPD of 43 kDa in size (XPD43) from Xanthomonas spp. is unusual as it lacks the strictly conserved tyrosine residue (equivalent to Tyr387 in Escherichia coli aminopeptidase P). XPD is ubiquitous in nature and has been isolated from mammals, bacteria, and archaea
-
evolution
-
XPD belongs to the M24B family of metalloenzymes. Xanthomonas spp. possess two different isoforms of XPD (48 and 43 kDa) which share about 24% sequence identity. The XPD of 43 kDa in size (XPD43) from Xanthomonas spp. is unusual as it lacks the strictly conserved tyrosine residue (equivalent to Tyr387 in Escherichia coli aminopeptidase P). XPD is ubiquitous in nature and has been isolated from mammals, bacteria, and archaea
-
malfunction
-
decreased serum prolidase activity and increased oxidative stress are correlated in early pregnancy loss, overview
malfunction
-
enzyme activity is increased in aortic dilatation compared to controls
malfunction
-
enzyme activity is increased in patients with nonalcoholic steatohepatitis, NASH, compared to controls, significant correlation between serum prolidase enzyme activity and fibrosis score in patients with NASH
malfunction
-
increased PSR activity in case of colitis
malfunction
misfunctioning causes prolidase deficiency, a recessive connective tissue disorder characterized by severe skin lesions, mental retardation and respiratory tract infections
malfunction
-
prolidase activity is significantly increased in patients with thalassemia major compared to the controls, relationship between prolidase activity and oxidative status in patients with thalassemia major, overview
malfunction
-
prolidase deficiency is a rare autosomal recessive disorder that affects the connective tissue. Symptoms of prolidase deficiency include skin lesions, mental retardation and recurrent respiratory infections. Prolidase is linked to collagen metabolism and is associated with melanoma. Prolidase is essential for collagen breakdown and the lack of this enzyme results in serious skin abnormalities. While an increase in prolidase activity and a decrease in collagen in breast cancer tissue may cause increased cancer risk. Recombinant human prolidase is used for enzyme replacement therapy
malfunction
-
prolidase deficiency is a rare, pan-ethnic, autosomal recessive disease with a broad phenotypic spectrum
malfunction
-
prolidase may play a role in angiogenesis
malfunction
-
serum prolidase activity and oxidative stress are significantly associated with the presence of etal growth restriction, the correlation between serum prolidase activity and markers of oxidative stress are represented as increased serum total oxidative status level and decreased serum total antioxidant capacity and total free sulfhydryl levels, suggesting an association of collagen turnover and oxidative stress in vascular dysfunction, overview
metabolism
-
prolidase catalyzes the final step of collagen degradation
metabolism
-
prolidase catalyzes the final step of collgane breakdown, releasing free proline for collagen recycling
metabolism
-
prolidase plays an important role in collagen metabolism, matrix remodeling and cell growth. Additionally, the final step of collagen degradation in the extracellular matrix is mediated by prolidase
metabolism
-
the enzyme is important in the collagen metabolism, overview
physiological function
-
OPAA-2 is active in detoxification of organophosphorus compounds, the nerve agents GB, sarin or O-isopropyl methylphosphonofluoridate, VX and blister agent HD, a sulfur mustard, overview
physiological function
-
prolidase activity may be a step-limiting factor in the regulation of collagen biosynthesis
physiological function
-
prolidase is a marker of collagen turnover. The enzyme activity is higher in women with early pregnancy loss than in those without. Collagen turnover is increased in patients with early pregnancy loss and may be an etiopathological factor of this disease
physiological function
-
prolidase is a specific imidodipeptidase involved in collagen degradation
physiological function
-
prolidase plays an important role in collagen metabolism, matrix remodeling and cell growth. Additionally, the final step of collagen degradation in the extracellular matrix is mediated by prolidase
physiological function
isozyme XPD43 is suggested to be important in the proton-shuttle transfer required for catalysis in the M24B (MEROPS) family
physiological function
-
isozyme XPD43 is suggested to be important in the proton-shuttle transfer required for catalysis in the M24B (MEROPS) family
-
physiological function
-
isozyme XPD43 is suggested to be important in the proton-shuttle transfer required for catalysis in the M24B (MEROPS) family
-
physiological function
-
isozyme XPD43 is suggested to be important in the proton-shuttle transfer required for catalysis in the M24B (MEROPS) family
-
physiological function
-
isozyme XPD43 is suggested to be important in the proton-shuttle transfer required for catalysis in the M24B (MEROPS) family
-
physiological function
-
isozyme XPD43 is suggested to be important in the proton-shuttle transfer required for catalysis in the M24B (MEROPS) family
-
physiological function
-
OPAA-2 is active in detoxification of organophosphorus compounds, the nerve agents GB, sarin or O-isopropyl methylphosphonofluoridate, VX and blister agent HD, a sulfur mustard, overview
-
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105000
-
2 * 105000, recombinant His-tagged enzyme, SDS-PAGE
120000 - 130000
-
gel filtration
123000
-
recombinant enzyme from Escherichia coli
132000
-
gradient gel electrophoresis
165000
-
gel filtration, prolidase II
185000
-
gel filtration, prolidase II from normal human and mother of patient with prolidase deficiencyr
210000
-
analytical ultracentrifugation
39400
-
2 * 39400, structure-function relationship, overview. The enzyme shows a pita-bread fold that encompasses a highly conserved metal center and substrate-binding pocket that is located in the enzymes C-terminal domain
40164
2 * 40000, recombinant enzyme, SDS-PAGE, 2 * 40164, mass spectrometry
42800
calculated from cDNA
50000
-
2 * 50000, SDS-PAGE
51000
-
2 * 51000, SDS-PAGE
53000
-
x * 58000, processed glycoslyated enzyme, SDS-PAGE, x * 53000, unprocessed enzyme, SDS-PAGE
57000
-
2 * 54305, sequence calculation, 2 * 55000-58000, native enzyme from different tissues, 2 * 56000, recombinant enzyme from Saccharomyces cerevisiae, 2 * 73000, recombinant enzyme from Pichia pastoris, 2 * 58000, recombinant enzyme from CHO cells, 2 * 57000, recombinant enzyme from Escherichia coli
64000
-
1 * 64000 + 1 * 68000, SDS-PAGE
68000
-
1 * 64000 + 1 * 68000, SDS-PAGE
68000 - 70000
-
gel filtration
80000
about, recombinant enzyme, gel filtration
95000
-
2 * 95000, SDS-PAGE, prolidase II from normal human and patients mother
additional information
-
hydrodynamic properties of wild-type and mutant DPP8s
100000
-
gel filtration
108000 - 116000
-
gel filtration
108000 - 116000
-
gel filtration
108000 - 116000
-
gel filtration
108000 - 116000
-
gel filtration, prolidase I from normal human and mother of patient with prolidase deficiency
40000
-
x * 40000, SDS-PAGE
40000
x * 40000, recombinant enzyme, SDS-PAGE
40000
2 * 40000, recombinant enzyme, SDS-PAGE, 2 * 40164, mass spectrometry
42000
-
x * 42000, SDS-PAGE
42000
-
2 * 42000, SDS-PAGE
54305
-
2 * 54305, calculation from DNA sequence
54305
-
2 * 54305, sequence calculation, 2 * 55000-58000, native enzyme from different tissues, 2 * 56000, recombinant enzyme from Saccharomyces cerevisiae, 2 * 73000, recombinant enzyme from Pichia pastoris, 2 * 58000, recombinant enzyme from CHO cells, 2 * 57000, recombinant enzyme from Escherichia coli
56000
-
SDS-PAGE
56000
-
native enzyme, SDS-PAGE
56000
-
x * 56000, SDS-PAGE
56000
-
2 * 56000, SDS-PAGE, prolidase I from normal human and mother of patient with prolidase deficiencyr
56000
-
2 * 54305, sequence calculation, 2 * 55000-58000, native enzyme from different tissues, 2 * 56000, recombinant enzyme from Saccharomyces cerevisiae, 2 * 73000, recombinant enzyme from Pichia pastoris, 2 * 58000, recombinant enzyme from CHO cells, 2 * 57000, recombinant enzyme from Escherichia coli
58000
-
x * 58000, SDS-PAGE
58000
-
2 * 58000, homodimerization via leucine zipper motif is required for activity, the active site is not required for dimerization
58000
-
x * 58000, processed glycoslyated enzyme, SDS-PAGE, x * 53000, unprocessed enzyme, SDS-PAGE
58000
-
x * 58000, recombinant enzyme, SDS-PAGE
58000
-
2 * 54305, sequence calculation, 2 * 55000-58000, native enzyme from different tissues, 2 * 56000, recombinant enzyme from Saccharomyces cerevisiae, 2 * 73000, recombinant enzyme from Pichia pastoris, 2 * 58000, recombinant enzyme from CHO cells, 2 * 57000, recombinant enzyme from Escherichia coli
70000
gel filtration
70000
recombinant enzyme, gel filtration
73000
-
x * 73000, SDS-PAGE
73000
-
2 * 54305, sequence calculation, 2 * 55000-58000, native enzyme from different tissues, 2 * 56000, recombinant enzyme from Saccharomyces cerevisiae, 2 * 73000, recombinant enzyme from Pichia pastoris, 2 * 58000, recombinant enzyme from CHO cells, 2 * 57000, recombinant enzyme from Escherichia coli
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multimer
-
x * 40000, SDS-PAGE
oligomer
-
x * 58000, SDS-PAGE
?
-
x * 73000, SDS-PAGE
?
-
x * 58000, processed glycoslyated enzyme, SDS-PAGE, x * 53000, unprocessed enzyme, SDS-PAGE
?
-
x * 58000, recombinant enzyme, SDS-PAGE
?
x * 40000, recombinant enzyme, SDS-PAGE
?
-
x * 40000, recombinant enzyme, SDS-PAGE
-
dimer
-
2 * 53000-58000, SDS-PAGE
dimer
-
1 * 64000 + 1 * 68000, SDS-PAGE
dimer
-
2 * 54305, calculation from DNA sequence
dimer
-
2 * 53000-58000, SDS-PAGE
dimer
-
2 * 56000, SDS-PAGE, prolidase I from normal human and mother of patient with prolidase deficiencyr
dimer
-
2 * 95000, SDS-PAGE, prolidase II from normal human and patient's mother
dimer
-
2 * 58000, homodimerization via leucine zipper motif is required for activity, the active site is not required for dimerization
dimer
-
2 * 105000, recombinant His-tagged enzyme, SDS-PAGE
dimer
-
2 * 54305, sequence calculation, 2 * 55000-58000, native enzyme from different tissues, 2 * 56000, recombinant enzyme from Saccharomyces cerevisiae, 2 * 73000, recombinant enzyme from Pichia pastoris, 2 * 58000, recombinant enzyme from CHO cells, 2 * 57000, recombinant enzyme from Escherichia coli
dimer
structure comparison to the enzyme from Pyrococcus horikoshii OT3 prolidase, overview
dimer
-
2 * 50000, SDS-PAGE
dimer
-
2 * 82000, SDS-PAGE
dimer
-
2 * 82000, SDS-PAGE
-
dimer
-
2 * 82000, SDS-PAGE
-
dimer
2 * 40000, recombinant enzyme, SDS-PAGE, 2 * 40164, mass spectrometry
dimer
-
2 * 40000, recombinant enzyme, SDS-PAGE, 2 * 40164, mass spectrometry
-
dimer
-
2 * 42000, SDS-PAGE
dimer
-
crystal structure
dimer
crystal structure, 2 subunits each with 2 domains, with the C-terminal domain bearing the active site
dimer
-
crystal structure analysis, active site analysis, overview
dimer
-
2 * 51000, SDS-PAGE
dimer
-
2 * 53000-58000, SDS-PAGE
dimer
2 * 42800, calculated
dimer
-
2 * 42800, calculated
-
dimer
-
2 * 42800, calculated
-
dimer
2 * 42800, about, sequence calculation
dimer
-
2 * 42800, about, sequence calculation
-
dimer
-
2 * 42800, about, sequence calculation
-
dimer
-
2 * 42800, about, sequence calculation
-
dimer
-
2 * 42800, about, sequence calculation
-
dimer
-
2 * 42800, about, sequence calculation
-
homodimer
-
-
homodimer
-
2 * 39400, structure-function relationship, overview. The enzyme shows a pita-bread fold that encompasses a highly conserved metal center and substrate-binding pocket that is located in the enzyme's C-terminal domain
monomer
-
-
monomer
-
1 * 41000, SDS-PAGE
additional information
-
The OPAA structure is composed of two domains, amino and carboxy domains, with the latter exhibiting a pita bread architecture and harboring the active site with the binuclear Mn2+ ions
additional information
-
The OPAA structure is composed of two domains, amino and carboxy domains, with the latter exhibiting a pita bread architecture and harboring the active site with the binuclear Mn2+ ions
-
additional information
-
enzyme contains a leucine zipper motif
additional information
-
molecular modeling
additional information
-
crystal structure and active site organization, overview
additional information
-
hydrodynamic properties of wild-type and mutant DPP8s, overview
additional information
molecular modeling, overview
additional information
-
molecular modeling, overview
-
additional information
formation of the standard dimer is structurally unstable in aqueous solution
additional information
-
formation of the standard dimer is structurally unstable in aqueous solution
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R46A
-
two orders of magnitude loss in the enzymatic activity for all the dipeptides attempted. The Glu340 side-chain interacts with Arg46 and stabilizes its side-chain conformation that is appropriate for substrate binding
A212P
-
naturally occuring mutation involved in prolidase deficiency
F822A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
G278D
-
naturally occuring point mutation causing prolidase deficiency
G448R
-
naturally occuring point mutation causing prolidase deficiency
H859A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
L368R
-
naturally occuring mutation involved in prolidase deficiency
R184Q
-
naturally occuring point mutation causing prolidase deficiency
R265X
-
naturally occuring point mutation causing prolidase deficiency
R276N
-
naturally occuring point mutation causing prolidase deficiency
V833A
-
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
Y231del
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homozygous mutation observed in two unrelated patients with enzyme deficiency. Mutation results in loss of enzyme activity in skin fibroblasts. Long-term cultured fibroblasts bearing the mutant accumulate Gly-L-Pro dipeptide intracellularly
Y256X
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a homozygous nonsense C > G transition at nucleotide 768 is a naturally occuring mutation, which leads to recalcitrant leg ulceration, splenomegaly, and photosensitive rash due to prolidase deficiency, phenotype, overview
Y844A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
L193E
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site-directed mutagenesis, the mutant is active on Pro-Pro in contrast to the wild-type enzyme, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme
L193E/V302D
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site-directed mutagenesis, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme
L193R
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site-directed mutagenesis, the mutation in the S1 site eliminates the allosteric behaviour of the enzyme, the mutant is active on Pro-Pro and Gly-Pro in presence of zinc ions in contrast to the wild-type enzyme, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme
L193R/V302D
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site-directed mutagenesis, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme
L193T
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site-directed mutagenesis, the mutant is active on Pro-Pro and Gly-Pro in contrast to the wild-type enzyme, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme
R293S
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the mutation results in the disappearance of the allosteric behaviour yielding a Hill constant of 0.98 while the wild type has a constant of 1.58 and suppresses the substrate inhibition that is observed in other mutants and wild type enzyme, the Km value for L-Leu-L-Pro is 2.9fold larger and Vmax is approximately 50% less as compared to the wild type enzyme
R293S/S307G
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mutant shows strongly reduced specific activity towards L-Leu-L-Pro compared to the wild type enzyme
S307D
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mutant shows reduced specific activity towards L-Leu-L-Pro compared to the wild type enzyme
S307G
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mutant shows reduced specific activity towards L-Leu-L-Pro compared to the wild type enzyme
S307R
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mutant shows reduced specific activity towards L-Leu-L-Pro compared to the wild type enzyme
V302D
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site-directed mutagenesis, the mutation in the S1 site eliminates the allosteric behaviour of the enzyme. The mutant is active on Pro-Pro in presence of zinc ions in contrast to the wild-type enzyme, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme
V302K
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site-directed mutagenesis, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme
V302T
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site-directed mutagenesis, the mutant shows altered substrate specificity and temperature profile compared to the wild-type enzyme
D209A
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less than 0.1% enzymic activity, contains 0.7 Co per subunit, maximal activity with 0.5 mM Co2+, less than 20% residual activity with 10 mM Co2+
E313L
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protein is highly misfolded, remains aggregated and recalcitrant during purification
E327L
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no enzymic activity, contains 0.03 Co per sunbunit
H284A
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less than 0.1% enzymic activity, protein is unfolded
H284L
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less than 0.1% enzymic activity, contains 0.28 Co per subunit. Inhibitory effect of high Co2+-concentration is less pronounced than in wild-type
R19G/K71E/S229
site-directed mutagenesis, the mutant shows altered kinetics and temperature profile
R19G/K71E/S229T
mutant enzyme shows a higher activity than wild-type enzyme over a broad range of temperatures, the thermostability of the mutant enzymes is less compared to wild type. At 35°C, 70°C and 100°C the mutant exhibits higher Vmax and kcat values than wild-type prolidase for Met-Pro. kcat/Km for Met-Pro is 1.1fold higher than wild-type value at 35°C, kcat/Km for Met -Pro comparable to wild-type value at 70°C, kcat/Km for Met-Pro is 2.4fold higher than wild-type value at 100°C. Relative specific activity towards Met-Pro at 100°C is 137% of wild-type activity. Relative specific activity towards Leu-Pro at 100°C is 169% of wild-type activity. Relative specific activity towards Phe-Pro at 100°C is 97% of wild-type activity. Relative specific activity towards Ala-Pro at 100°C is 95% of wild-type activity. Relative specific activity towards Gly-Pro at 100°C is 47% of wild-type activity. Relative specific activity towards Arg-Pro at 100°C is 101% of wild-type activity. Catalytic activity of the mutant enzyme has similar response to changes in pH as wild-type enzyme and shows optimal activity at pH 7.0, although the activity is 89% of wild-type activity
A195T/G306S
mutation causes an increase in Tm-value of 0.1°C. Mutation causes an 1.7fold increase of the catalytic efficiency towards Leu-Pro
E127G/E252D
mutation causes an decrease in Tm-value of 2.1°C. Mutation causes an 1.3fold increase of the catalytic efficiency towards Leu-Pro
E36V
mutation causes an increase in Tm-value of 0.6°C. Mutation causes an 1.1fold increase of the catalytic efficiency towards Leu-Pro
Y301C/K342N
mutation causes an decrease in Tm-value of 0.5°C. Mutation causes an 1.2fold decrease of the catalytic efficiency towards Leu-Pro
A195T/G306S
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mutation causes an increase in Tm-value of 0.1°C. Mutation causes an 1.7fold increase of the catalytic efficiency towards Leu-Pro
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E127G/E252D
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mutation causes an decrease in Tm-value of 2.1°C. Mutation causes an 1.3fold increase of the catalytic efficiency towards Leu-Pro
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E36V
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mutation causes an increase in Tm-value of 0.6°C. Mutation causes an 1.1fold increase of the catalytic efficiency towards Leu-Pro
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Y301C/K342N
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mutation causes an decrease in Tm-value of 0.5°C. Mutation causes an 1.2fold decrease of the catalytic efficiency towards Leu-Pro
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S202F
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naturally occuring point mutation causing prolidase deficiency
S202F
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naturally occuring mutation involved in prolidase deficiency
G39E
site-directed mutagenesis, the mutant shows altered kinetics and temperature profile
G39E
at 35°C, 70°C and 100°C the mutant exhibits higher Vmax and kcat values than wild-type prolidase for Met-Pro. kcat/Km for Met-Pro is 70% of wild-type value at 35°C, kcat/Km for Met-Pro is 80% of wild-type value at 70°C, kcat/Km for Met-Pro is 1.2fold higher than wild-type value at 100°C. Relative specific activity towards Met-Pro at 100°C is 103% of wild-type activity. Relative specific activity towards Leu-Pro at 100°C is 85% of wild-type activity. Relative specific activity towards Phe-Pro at 100°C is 60% of wild-type activity. Relative specific activity towards Ala-Pro at 100°C is 35% of wild-type activity. Relative specific activity towards Gly-Pro at 100°C is 37% of wild-type activity. Relative specific activity towards Arg-Pro at 100°C is 132% of wild-type activity. Catalytic activity of the mutant enzyme has similar response to changes in pH as wild-type enzyme and shows optimal activity at pH 6.0, although the activity is 60% of wild-type activity
R19G/G39E/K71E/S229T
site-directed mutagenesis, the mutant shows altered kinetics and temperature profile
R19G/G39E/K71E/S229T
mutant enzyme shows a higher activity than wild-type enzyme over a broad range of temperatures, the thermostability of the mutant enzymes is less compared to wild type. At 35°C, 70°C and 100°C the mutant exhibits higher Vmax and kcat values than wild-type prolidase for Met-Pro. kcat/Km for Met-Pro is 1.2fold higher than wild-type value at 35°C, kcat/Km for Met -Pro is 1.8fold higher than wild-type value at 70°C, kcat/Km for Met-Pro is 2.5fold higher than wild-type value at 100°C. Relative specific activity towards Met-Pro at 100°C is 143% of wild-type activity. Relative specific activity towards Leu-Pro at 100°C is 79% of wild-type activity. Relative specific activity towards Phe-Pro at 100°C is 122% of wild-type activity. Relative specific activity towards Ala-Pro at 100°C is 38% of wild-type activity. Relative specific activity towards Gly-Pro at 100°C is 10% of wild-type activity. Relative specific activity towards Arg-Pro at 100°C is 112% of wild-type activity
additional information
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construction and expression of leucine zipper mutants and active site mutants, the former show no remaining activity, while the latter are not catalytically active but are still able to dimerize
additional information
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complete map of the known PEPD mutant alleles causing prolidase deficiency, which is a rare recessive disorder characterized by severe skin lesions, single amino acid substitutions, exon splicing, deletions and a duplication are described as causative for the disease and are mainly located at highly conserved amino acids in the sequence of prolidase, genotype-phenotype correlation, clinical phenotype, overview
additional information
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enzyme decficiency leads to a rare autosomal recessive disease, characterized by a wide range of clinical outcomes, including severe skin lesions, mental retardation, and infections of the respiratory tract, genotype/phenotype relationship, overview
additional information
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identification of 17 mutations involved in prolidase deficiency, a rare, pan-ethnic, autosomal recessive disease with a broad phenotypic spectrum. Phenotypes of 20 prolidase deficient patients of Arab Moslem and Druze origin from 10 kindreds residing in northern Israel, overview
additional information
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the use of Pyrococcus furiosus prolidase for organophosphorus nerve agent decontamination is restricted by the fact that this enzyme displays a narrow functional temperature range. Like many other enzymes isolated from hyperthermophiles, Pyrococcus furiosus prolidase has only 50% activity at 80°C and displays little activity at temperatures below 50°C. Therefore a random-mutated Pyrococcus furiosus prolidase gene library is constructed and screened for production of mutants with increased activity at room temperature while maintaining thermostability. The mutant enzyme shows increased activity over the pH range of 57. At pH 5.0, the mutant activity is 1.6fold higher than wild-type activity, and at pH 7.0, it is 1.2fold higher than wild type
additional information
the use of Pyrococcus furiosus prolidase for organophosphorus nerve agent decontamination is restricted by the fact that this enzyme displays a narrow functional temperature range. Like many other enzymes isolated from hyperthermophiles, Pyrococcus furiosus prolidase has only 50% activity at 80°C and displays little activity at temperatures below 50°C. Therefore a random-mutated Pyrococcus furiosus prolidase gene library is constructed and screened for production of mutants with increased activity at room temperature while maintaining thermostability. The mutant enzyme shows increased activity over the pH range of 57. At pH 5.0, the mutant activity is 1.6fold higher than wild-type activity, and at pH 7.0, it is 1.2fold higher than wild type
additional information
randomly mutated enzymes are prepared Tt obtain a better enzyme for organophosphorus nerve agent decontamination and to investigate the structural factors that may influence protein thermostability and thermoactivity
additional information
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randomly mutated enzymes are prepared Tt obtain a better enzyme for organophosphorus nerve agent decontamination and to investigate the structural factors that may influence protein thermostability and thermoactivity
additional information
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randomly mutated enzymes are prepared Tt obtain a better enzyme for organophosphorus nerve agent decontamination and to investigate the structural factors that may influence protein thermostability and thermoactivity
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analysis
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applications using prolidase to detoxify organophosphorous compounds nerve agents include its incorporation into fire-fighting foams and as biosensors for organophosphorous compound detection
biotechnology
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the enzyme is of particular interest because it can be used in many biotechnological applications
degradation
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advantages of using Alteromonas recombinant prolidase in biodecontamination foams due to its high activity against G-type nerve agents, such as soman and sarin
degradation
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prolidase is able to degrade toxic organophosphorus compounds, namely, by cleaving the P-F and P-O bonds in the nerve agents, sarin and soman. Applications using prolidase to detoxify organophosphorous nerve agents include its incorporation into fire-fighting foams and as biosensors for organophosphorous compound detection
degradation
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advantages of using Alteromonas recombinant prolidase in biodecontamination foams due to its high activity against G-type nerve agents, such as soman and sarin
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diagnostics
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cord blood prolidase activity may be a good indicator of fetal maturation and gestational age
diagnostics
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prolidase might be a useful marker for the diagnosis of lymphoma
diagnostics
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prolidase activity may be a useful adjunctive tool in predicting liver fibrosis, especially in the absence of advanced fibrosis and other conditions, which may affect the interpretation of prolidase activity
diagnostics
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prolidase is a marker of collagen turnover
diagnostics
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prolidase is a potential biomarker for melanoma, and the enzyme is a target for drug development in cancer therapy
drug development
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the enzyme is a target in breast cancer therapy
drug development
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the enzyme is used as target enzyme for specific melanoma prodrug activation
drug development
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prolidase is a potential biomarker for melanoma, and the enzyme is a target for drug development in cancer therapy
food industry
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prolidase can be used in dietary industry as bitterness reducing agent
food industry
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prolidases are employed in the cheese-ripening process to improve cheese taste and texture
food industry
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prolidases are employed in the cheese-ripening process to improve cheese taste and texture
food industry
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prolidases are employed in the cheese-ripening process to improve cheese taste and texture
food industry
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prolidases are employed in the cheese-ripening process to improve cheese taste and texture
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medicine
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enzyme is a possible target for doxycyclin-induced inhibition of collagen synthesis in the treatment of osteoarthritis
medicine
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elevated pH-value in vaginal fluid accompanied by high sialidase and high enzyme activity are associated with low and verly low birth weight and early preterm at less than 35 or 32 weeks gestation
medicine
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enzyme activity in normal human erythrocyte is strongly enhanced by Gly, L-Ala, L-Ser with MnCl2 and enhanced by D-Leu and D-Val. L-Val and L-Leu are strong inhibitors. Enzyme activity in a patient with enzyme deficiency is also enhanced by Gly, L-Ala, and L-Ser and by D-Leu and L-Val, L-Leu is inhibitory
medicine
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no statistical difference in serum enzyme activity between postmenopausal osteoporotic, postmenopausal nonosteoporotic and premenopausal healthy women. No significant correlations between serum enzyme level and any biomarkers of bone turnover as well as bone mineral density
medicine
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patients with severe phenotype of enzyme deficiency showing infection, hepatosplenomegaly, thrombocytopenia, classic skin ulcers, and multisystem involvement. Enzyme activity in patients is nearly undetectable due to a single nucleotide mutation c.793 T>C in exon 11, resulting in a premature stop codon at amino acid residue 265
medicine
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teloid tissue shows up to 4fold increase in enzyme activity compared to normal skin. Elevated enzyme activity is accompanied by increase in concentrations of aminoterminal propeptide of type I procollagen and carboxyterminal telopeptide of type I collagen and increased collagen turnover index
medicine
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prolidase activity in bronchial asthma and pathogenesis is significant as a collagen turnover indicator and can be used in both to evaluate pathogenesis and prognosis
medicine
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prolidase-loaded chitosan nanoparticles permit to restore prolidase activity in prolidase deficiency fibroblasts for 8 days
medicine
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serum prolidase activity is significantly associated with the presence and severity of coronary artery disease, elevated serum prolidase activity may be an independent predictor of coronary atherosclerosis
medicine
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the presence of atrial fibrillation in patients with severe mitral stenosis may be associated with the plasma prolidase activity
medicine
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the serum prolidase enzyme activity of patients with steatohepatitis is significantly increased compared with the patients with simple steatosis and controls, serum prolidase enzyme activity is positively correlated with the grade of liver fatty infiltration, lobular inflammation, non-alcoholic fatty liver disease activity score, and stage of fibrosis, serum prolidase enzyme activity is the best predictor for distinguishing steatohepatitis from simple steatosis
medicine
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Recombinant human prolidase is used for enzyme replacement therapy in prolidase deficiency