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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
-
-
?