3.4.21.26: prolyl oligopeptidase
This is an abbreviated version!
For detailed information about prolyl oligopeptidase, go to the full flat file.
Word Map on EC 3.4.21.26
-
3.4.21.26
-
dipeptidyl
-
stroma
-
cancer-associated
-
aminopeptidase
-
neuropeptides
-
endopeptidases
-
neurotensin
-
proline-containing
-
fapis
-
biodistribution
-
myofibroblasts
-
flavobacterium
-
celiac
-
beta-propeller
-
bradykinin
-
trh
-
dppiv
-
meningosepticum
-
3.4.14.5
-
18f-fdg
-
theranostic
-
exopeptidase
-
pyroglutamyl
-
phosphoramidon
-
amanita
-
amnesia
-
carcinoma-associated
-
peptidase-iv
-
pharmacology
-
ac-sdkp
-
seven-bladed
-
gluten-free
-
suvmean
-
gliadin
-
n-acetyl-seryl-aspartyl-lysyl-proline
-
bispecific
-
acylpeptide
-
medicine
-
nutrition
-
food industry
-
drug development
- 3.4.21.26
-
dipeptidyl
-
stroma
-
cancer-associated
- aminopeptidase
- neuropeptides
- endopeptidases
- neurotensin
-
proline-containing
-
fapis
-
biodistribution
-
myofibroblasts
- flavobacterium
- celiac
-
beta-propeller
- bradykinin
- trh
- dppiv
- meningosepticum
-
3.4.14.5
-
18f-fdg
-
theranostic
-
exopeptidase
-
pyroglutamyl
- phosphoramidon
- amanita
- amnesia
-
carcinoma-associated
-
peptidase-iv
- pharmacology
-
ac-sdkp
-
seven-bladed
-
gluten-free
-
suvmean
- gliadin
-
n-acetyl-seryl-aspartyl-lysyl-proline
-
bispecific
-
acylpeptide
- medicine
- nutrition
- food industry
- drug development
Reaction
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides =
Synonyms
apPEP, cyproase I, EC 3.4.22.18, endoprolylpeptidase, eryngase, FAP, fibroblast activation protein, FlaP, glutenase, membrane-bound PE, More, mPOP, PE, PEP, PepO2, peptidase, postproline endo-, POP, POP Tb, POP Tc80, POPA, POPB, post proline cleaving enzyme, post prolyl cleaving enzyme, post-proline cleaving endopeptidase, post-proline cleaving enzyme, post-proline cutting enzyme, post-proline endopeptidase, postproline cleaving enzyme, postproline endopeptidase, postproline-cleaving enzyme, PPCE, PREP, PREPL A, proline endopeptidase, proline specific prolyl endopeptidase, proline-specific endopeptidase, proly endopeptidase, prolyl endopeptidase, prolyl endoprotease, prolyl oligopeptidase, prolyl oligopeptidase B, prolylendopeptidase, prost-proline cleaving enzyme, PsE, S28A, S28B, TNA1_POP
ECTree
3.4.21.26 prolyl oligopeptidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.21.26 - prolyl oligopeptidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-benzyl 2-(2-(4-hydroxynaphthalen-1-ylcarbamoyl)pyrrolidin-1-yl)-2-oxoethylcarbamate + H2O
?
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro + Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
the fluorescence resonance energy transfer peptide sequence corresponds to bradykinin from human kininogen
-
-
?
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro + Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
the fluorescence resonance energy transfer peptide sequence corresponds to bradykinin from human kininogen
-
-
?
2-aminobenzoyl-FFQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
-
-
-
?
2-aminobenzoyl-FPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
2-aminobenzoyl-FP + Q-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
2-aminobenzoyl-FSQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
-
-
-
?
2-aminobenzoyl-Glu-Gly-L-Phe-Gly-L-Pro-L-Phe-Gly-L-4-nitrophenylalanine-L-Ala + H2O
2-aminobenzoyl-Glu-Gly-L-Phe-Gly-L-Pro + L-Phe-Gly-L-4-nitrophenylalanine-L-Ala
-
-
-
-
?
2-aminobenzoyl-Glu-Gly-Phe-Ser-Pro-Phe(NO2)-Arg-Ala + H2O
2-aminobenzoyl-Glu-Gly-Phe-Ser-Pro + Phe(NO2)-Arg-Ala
-
-
?
2-aminobenzoyl-Glu-Phe-Ser-Pro-Phe(NO2)-Arg-Ala + H2O
2-aminobenzoyl-Glu-Phe-Ser-Pro + Phe(NO2)-Arg-Ala
-
-
?
2-aminobenzoyl-Gly-Glu-Ser-Pro-Phe(NO2)-Arg-Ala + H2O
2-aminobenzoyl-Gly-Glu-Ser-Pro + Phe(NO2)-Arg-Ala
-
-
?
2-aminobenzoyl-Gly-L-Phe-Gly-L-Pro-L-Phe-Gly-L-4-nitrophenylalanine-L-Ala + H2O
2-aminobenzoyl-Gly-L-Phe-Gly-L-Pro + L-Phe-Gly-L-4-nitrophenylalanine-L-Ala
-
-
-
-
?
2-aminobenzoyl-Gly-L-Phe-L-Arg-L-Pro-L-4-nitrophenylalanine-L-Arg-L-Ala + H2O
2-aminobenzoyl-Gly-L-Phe-L-Arg-L-Pro + L-4-nitrophenylalanine-L-Arg-L-Ala
-
-
-
-
?
2-aminobenzoyl-Gly-Phe-Arg-Pro-Phe(NO2)-Arg-Ala + H2O
2-aminobenzoyl-Gly-Phe-Arg-Pro + Phe(NO2)-Arg-Ala
-
-
?
2-aminobenzoyl-Gly-Phe-Glu-Pro-Phe(NO2)-Arg-Ala + H2O
2-aminobenzoyl-Gly-Phe-Glu-Pro + Phe(NO2)-Arg-Ala
-
-
?
2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala-NH2 + H2O
2-aminobenzoyl-Gly-Phe-Gly-Pro + Phe-Gly-Phe(NO2)-Ala-NH2
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gly-Phe-Ser-Pro + Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
a fluorescence resonance energy transfer peptide
-
-
?
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gly-Phe-Ser-Pro + Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
the fluorescence resonance energy transfer peptide sequence corresponds to bradykinin from human kininogen
-
-
?
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Ile-Gly-GLu-Ile-Lys-Glu-Glu-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gly-Phe-Ser-Pro + Phe-Arg-Ser-Ser-Arg-Ile-Gly-GLu-Ile-Lys-Glu-Glu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
the fluorescence resonance energy transfer peptide sequence corresponds to bradykinin from human kininogen
-
-
?
2-aminobenzoyl-Gly-Pro-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gly-Pro + Gln-N-(2,4-dinitrophenyl)ethylenediamine
2-aminobenzoyl-Gly-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gly-Pro + Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
a fluorescence resonance energy transfer peptide
-
-
?
2-aminobenzoyl-Gly-Pro-Phe-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gly-Pro + Phe-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
a fluorescence resonance energy transfer peptide
-
-
?
2-aminobenzoyl-Gly-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gly-Ser-Pro + Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
a fluorescence resonance energy transfer peptide
-
-
?
2-aminobenzoyl-L-Ser-L-Pro-L-4-nitrophenylalanine-L-Ala + H2O
2-aminobenzoyl-L-Ser-L-Pro + 4-nitrophenylalanine-L-Ala
-
-
-
-
?
2-aminobenzoyl-RPPGFQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
-
-
-
?
2-aminobenzoyl-RPPGFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
2-aminobenzoyl-RPP + GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
-
-
?
2-aminobenzoyl-SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
-
-
-
?
4-((4-(dimethylamino)phenyl)azo)benzoyl-GPQGLLGA-L-glutamyl-gamma-(2-(1-sulfonyl-5-naphthyl)-aminoethylamide)-NH2 + H2O
?
-
-
-
-
?
Abz-Gly-L-Phe-L-Arg-L-Pro-L-Phe(NO2)-L-Arg-L-Ala + H2O
Abz-Gly-L-Phe-L-Arg-L-Pro + L-Phe(NO2)-L-Arg-L-Ala
-
-
-
-
?
Abz-Gly-L-Phe-L-Ser-L-Pro-L-Phe-L-Arg-L-Ser-L-Ser-L-Arg-L-Ile-Gly-L-Glu-L-Ile-L-Lys-L-Glu-L-Glu-L-Gln-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
Abz-Gly-L-Phe-L-Ser-L-Pro + L-Phe-L-Arg-L-Ser-L-Ser-L-Arg-L-Ile-Gly-L-Glu-L-Ile-L-Lys-L-Glu-L-Glu-L-Gln-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
AbzGFGPFGF(p-NO2)A-NH2 + H2O
AbzGFGP + FGF(p-NO2)A-NH2
-
assay at pH 8.0, 37°C, reaction stopped by heating at 95°C for 5 min
-
-
?
Ac-CDPGYIGSR-NH2 + H2O
?
-
substrate specificity studies on membrane PE as compared with POP. ZPP-sensitive cleavage of both occurred
-
-
?
Ala-Gly-Pro-beta-naphthylamide + H2O
Ala-Gly-Pro + 2-naphthylamine
Lyophyllum cinerascens
-
-
-
?
alpa2-antiplasmin + H2O
?
-
not a robust substrate in vitro, the enzyme cleaves after Pro12 in the T9S10G11P12-N13 Q14E15Q16E17 sequence
-
-
?
alpha-melanocyte-stimulating hormone + H2O
acetyl-SYSMEHFRWGKP + L-Val
acetyl-SYSMEHFRWGKPV
-
-
?
alpha-MSH(1-13) + H2O
alpha-MSH(1-12) + Pro
-
increased ratio between substrate and product in pituitaries of prolyl endopeptidase deficient mice compared to wild type mice
-
-
?
alpha-synulein + H2O
?
-
the enzyme binds to alpha-synuclein and enhances its dimerization
-
-
?
alpha2-gliadin 33-mer + H2O
?
-
the enzyme is able to break down 63% of the 33-mer after 8 h of incubation and it is almost completely degraded after 12 h
-
-
?
benzyloxycarbonyl-Ala-Ala-4-nitroanilide + H2O
benzyloxycarbonyl-Ala-Ala + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Ala + beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Ala-Ala-p-nitroanilide + H2O
benzyloxycarbonyl-Ala-Ala + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-Ala-Ala-p-nitrophenol + H2O
benzyloxycarbonyl-Ala-Ala + p-nitrophenol
-
-
-
?
benzyloxycarbonyl-Ala-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Gly-Pro + beta-naphthylamine
benzyloxycarbonyl-Ala-Gly-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Ala-Gly-Pro + p-nitrophenol
-
enzyme from kidney
-
?
benzyloxycarbonyl-Ala-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Ala-Pro + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Ala-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Pro + beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Ala-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Ala-Pro + p-nitrophenol
-
enzyme from kidney
-
?
benzyloxycarbonyl-D-Ala-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-D-Ala-Gly-Pro + beta-naphthylamine
benzyloxycarbonyl-D-Ala-Gly-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-D-Ala-Gly-Pro + p-nitrophenol
-
enzyme from kidney
-
?
benzyloxycarbonyl-D-Ala-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-D-Ala-Pro + beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Gly-Gly-Pro + p-nitrophenol
benzyloxycarbonyl-Gly-L-Pro-2-naphthylamide + H2O
benzyloxycarbonyl-Gly-L-Pro + 2-naphthylamine
-
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-L-Pro + 4-nitroaniline
benzyloxycarbonyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-L-Pro + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Gly-L-Pro-doxorubicin + H2O
benzyloxycarbonyl-Gly-L-Pro + doxorubicin
-
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-melphalan + H2O
benzyloxycarbonyl-Gly-L-Pro + melphalan
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-2-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + 2-naphthylamine
benzyloxycarbonyl-Gly-Pro-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
benzyloxycarbonyl-Gly-Pro-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Gly-Pro + 4-nitrophenol
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + 2-naphthylamine
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + beta-naphthylamine
benzyloxycarbonyl-Gly-Pro-D-Ala + H2O
benzyloxycarbonyl-Gly-Pro + D-Ala
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-D-Leu + H2O
benzyloxycarbonyl-Gly-Pro + D-Leu
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly-D-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Gly-D-Ala
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-SBzl + H2O
benzyloxycarbonyl-Gly-Pro + phenyl-methanethiol
-
-
?
benzyloxycarbonyl-Gly-Pro-thiobenzyl ester + H2O
benzyloxycarbonyl-Gly-Pro + phenylmethanethiol
-
-
-
-
?
benzyloxycarbonyl-glycyl-l-prolyl-4-nitroanilide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Pro + p-nitrophenol
-
enzyme from kidney
-
?
beta-endorphin + h2O
Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro + Leu-Val-Thr-Leu-Phe-Lys-Asn-Ala + Ile-Ile-Lys-Asn-Ala + Tyr-Lys-Lys-Gly-Glu
-
-
-
?
bradykinin + H2O
Arg-Pro-Pro + Gly-Phe-Ser-Pro + Phe-Arg
-
-
-
?
collagen + H2O
N-acetyl-Pro-Gly-Pro + ?
-
after enzyme activation with LPS
-
-
?
fish muscle collagen + H2O
?
-
the enzyme hydrolysis site is at the carboxyl terminus of prolyl residues
-
-
?
FVNEHLCGSHLVQALTLVCGQRGFFYTPLA + H2O
FVNEHLCGSHLVQALTLVCGQRGFFYTP + LA
-
-
-
?
Gliadin + H2O
?
-
digestion of the gliadin peptide in short peptides with both enzymes S28A and S28B, occur from its N terminus
-
-
?
Gly-L-Pro-7-amido-4-methylcoumarin + H2O
Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-4-methoxy-beta-naphthylamide + H2O
Gly-Pro + 4-methoxy-beta-naphthylamine
-
-
-
-
?
GnRH + H2O
pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro + Gly-NH2
-
-
-
?
H-(O2Oc)2-K(Abz)GFGPFGF(p-NO2)A-NH2 + H2O
?
-
assay at pH 8.0, 37°C, reaction stopped by heating at 95°C for 5 min
-
-
?
H-Abz-GFGP-OH + H2O
?
-
assay at pH 8.0, 37°C, reaction stopped by heating at 95°C for 5 min
-
-
?
H-Abz-GFGPFGF(p-NO2)A-NH2 + H2O
?
-
assay at pH 8.0, 37°C, reaction stopped by heating at 95°C for 5 min
-
-
?
H-F(p-NO2)GFGP-OH + H2O
?
-
assay at pH 8.0, 37°C, reaction stopped by heating at 95°C for 5 min
-
-
?
H-F(p-NO2)GFGPFGK(Abz)A-(O2Oc)-HMBA-PEGA + H2O
H-F(p-NO2)GFGP + FGK(Abz)A-(O2Oc)-HMBA-PEGA
-
assay at pH 8.0, 37°C, reaction stopped by heating at 95°C for 5 min
-
-
?
H-F(p-NO2)GFGPFGK(Abz)A-(O2Oc)-NH2 + H2O
H-F(p-NO2)GFGP + FGK(Abz)A-(O2Oc)-NH2
-
assay at pH 8.0, 37°C, reaction stopped by heating at 95°C for 5 min
-
-
?
H-F(p-NO2)GFGPFGK(Abz)A-(O2Oc)2-HMBA-PEGA + H2O
H-F(p-NO2)GFGP + FGK(Abz)A-(O2Oc)2-HMBA-PEGA
-
assay at pH 8.0, 37°C, reaction stopped by heating at 95°C for 5 min
-
-
?
H-F(p-NO2)GFGPFGK(Abz)A-(O2Oc)2-NH2 + H2O
H-F(p-NO2)GFGP + FGK(Abz)A-(O2Oc)2-NH2
-
assay at pH 8.0, 37°C, reaction stopped by heating at 95°C for 5 min
-
-
?
H-F(p-NO2)GFGPFGK(Abz)A-HMBA-PEGA + H2O
H-F(p-NO2)GFGP + FGK(Abz)A-HMBA-PEGA
-
assay at pH 8.0, 37°C, reaction stopped by heating at 95°C for 5 min
-
-
?
H-F(p-NO2)GFGPFGK(Abz)A-NH2 + H2O
H-F(p-NO2)GFGP + FGK(Abz)A-NH2
-
assay at pH 8.0, 37°C, reaction stopped by heating at 95°C for 5 min
-
-
?
H-FGF(p-NO2)A-NH2 + H2O
?
-
assay at pH 8.0, 37°C, reaction stopped by heating at 95°C for 5 min
-
-
?
H-K(Abz)-GFGPFGF(p-NO2)A-NH2 + H2O
?
-
assay at pH 8.0, 37°C, reaction stopped by heating at 95°C for 5 min
-
-
?
H-MDPVDPNIE-OH + H2O
?
-
substrate specificity studies on membrane PE as compared with POP. ZPP-sensitive cleavage of both occurred
-
-
?
H-O2Oc-K(Abz)-GFGPFGF(p-NO2)A-NH2 + H2O
?
-
assay at pH 8.0, 37°C, reaction stopped by heating at 95°C for 5 min
-
-
?
H2N-QLQPFPQPQLPY-OH + H2O
?
-
substrate specificity studies on membrane PE as compared with POP. ZPP-sensitive cleavage of both occurred
-
-
?
IWGIGCNPWTAEHVDQTLASGNDIC + H2O
cyclic IWGIGCNP + WTAEHVDQTLASGNDIC
-
a peptide with 25 amino acids (25mer, sequence IWGIGCNPWTAEHVDQTLASGNDIC) is utilized by the enzyme as a substrate for the macrocyclization reaction. During the macrocyclase reaction, the enzyme generates an eight-amino acid cyclic peptide from the N-terminal residues (the core, sequence IWGIGCNP), cleaving off the 17-C-terminal amino acid recognition sequence (peptide tail, sequence WTAEHVDQTLASGNDIC)
-
-
?
L-Ala-L-Ala-L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala-L-Ala-L-Ala-L-Pro + 4-nitroaniline
-
-
-
-
?
L-Ala-L-Pro-L-Pro-4-nitroanilide + H2O
L-Ala-L-Pro-L-Pro + 4-nitroaniline
-
-
-
-
?
L-Tyr-4-nitroanilide + H2O
L-Tyr + 4-nitroaniline
-
second best substrate
-
-
?
luteinizing-hormone-releasing hormone + H2O
pEHWSYGLRP + Gly
pEHWSYGLRPG
-
-
?
Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Lys-Arg-Pro-Pro + Gly-Phe-Ser-Pro-Phe-Arg
-
as active as potentiator B
-
?
Me-O-succinyl-Ala-Ala-Val p-nitroanilide + H2O
Me-O-succinyl-Ala-Ala + Val p-nitroanilide
-
-
-
?
membrane-associated glycoprotein neural cell adhesion molecule + H2O
?
-
-
-
-
?
Met-Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Met-Lys-Arg-Pro-Pro + Gly-Phe-Ser-Pro-Phe-Arg
-
as active as potentiator B
-
?
N-benzyloxycarbonyl-Ala-Ala-p-nitrophenyl ester + H2O
?
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-4-nitrophenyl ester + H2O
N-benzyloxycarbonyl-Gly-Pro + 4-nitrophenol
N-benzyloxycarbonyl-Gly-Pro-p-nitrophenyl ester + H2O
?
-
-
-
-
?
N-carbobenzoxy-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
N-carbobenzoxy-Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
N-carbobenzyloxy-glycyl-proline-4-methyloumarin-7-amide + H2O
N-carbobenzyloxy-glycyl-proline + 7-amino-4-methylcoumarin
-
-
-
-
?
N-Suc-Ala-Ala-Ala-7-amido-4-methylcoumarin + H2O
N-Suc-Ala-Ala-Ala + 7-amino-4-methylcoumarin
assay at pH 7.5, 25°C
-
-
?
N-Suc-Gly-Pro-7-amido-4-methylcoumarin + H2O
N-Suc-Gly-Pro + 7-amino-4-methylcoumarin
assay at pH 7.5, 25°C
-
-
?
N-Suc-Gly-Pro-Leu-Gly-Pro-7-amido-4-methylcoumarin + H2O
N-Suc-Gly-Pro-Leu-Gly-Pro + 7-amino-4-methylcoumarin
assay at pH 7.5, 25°C
-
-
?
N-succinyl-Ala-Ala-Ala-4-nitroanilide
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
-
-
-
-
?
N-succinyl-Ala-Pro-4-nitroanilide + H2O
N-succinyl-Ala-Pro + 4-nitroaniline
-
-
-
?
N-succinyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
?
24% of the activity with N-succinyl-Gly-L-Pro-L-Leu-Gly-L-Pro-7-amido-4-methylcoumarin
-
-
?
N-succinyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
N-succinyl-Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
N-succinyl-Gly-L-Pro-L-Leu-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
N-succinyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
N-succinyl-Gly-Pro + 7-amino-4-methylcoumarin
N-succinyl-glycyl-proline-4-methylcoumarin-7-amide + H2O
N-succinyl-glycyl-proline + 7-amino-4-methylcoumarin
N-succinyl-glycyl-prolyl-7-amido-4-methylcoumarin + H2O
N-succinyl-glycyl-prolyl + 7-amino-4-methylcoumarin
N-succinyl-L-Ala-L-Ala-L-Ala-7-amido-4-methylcoumarin + H2O
?
13% of the activity with N-succinyl-Gly-L-Pro-L-Leu-Gly-L-Pro-7-amido-4-methylcoumarin
-
-
?
neurotensin + H2O
pGlu-Leu-Tyr-Glu-Asn-Lys-Pro + Arg-Arg-Pro + Tyr-Ile-Leu
-
-
-
?
PEGA(O2Oc)2-K(Abz)GFGPFGF(p-NO2)A-NH2 + H2O
?
-
assay at pH 8.0, 37°C, reaction stopped by heating at 95°C for 5 min
-
-
?
PEGA-K(ABz)-GFGPFGF(p-NO2)A-NH2 + H2O
?
-
assay at pH 8.0, 37°C, reaction stopped by heating at 95°C for 5 min
-
-
?
PEGA-O2Oc-K(Abz)GFGPFGF(p-NO2)A-NH2 + H2O
?
-
assay at pH 8.0, 37°C, reaction stopped by heating at 95°C for 5 min
-
-
?
peptide QATVGDVNTDRPGLLDLK + H2O
TVGDVNTDRPGLLDLK + GDVNTDRPGLLDLK + QA + QATV
-
i.e. octadecaneuropeptide ODN, the biologically active fragment of diazepam-binding inhibitor, the Ala2 residue is preferred by the enzyme for cleavage, while the Pro-Gly bind is not cleaved, overview
-
-
?
pGlu-Gly-Leu-Pro-Pro-Arg-Pro + H2O
pGlu-Gly-Leu-Pro-Pro + Arg-Pro
-
i.e. potentiator B
-
?
pGlu-Gly-Leu-Pro-Pro-Gly-Pro + H2O
pGlu-Gly-Leu-Pro-Pro + Gly-Pro
-
i.e. potentiator C, as active as potentiator B
-
?
polysialylated membrane-associated glycoprotein neural cell adhesion molecule + H2O
?
-
-
-
-
?
RPPGFSPFR + H2O
?
-
i.e. bradykinin, 90% of the activity with potentiator B, i.e. pGlu-Gly-Leu-Pro-Pro-Arg-Pro
-
?
RPPGFSPFR-amide + H2O
RPP + GFSPFR-amide
-
i.e. bradykinin, 70% of the activity with potentiator B, i.e. pGlu-Gly-Leu-Pro-Pro-Arg-Pro
-
?
succinyl-D-Ala-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-D-Ala-Pro + 4-nitroaniline
-
-
-
-
?
succinyl-Gly-L-Pro-4-nitroanilide + H2O
succinyl-Gly-L-Pro + 4-nitroaniline
-
-
-
-
?
succinyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
succinyl-Gly-L-Pro + 7-amino-4-methylcoumarin
succinyl-Gly-L-Pro-L-Leu-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
succinyl-Gly-L-Pro-L-Leu-Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Gly-Pro-4-methylcoumaryl-7-amide + H2O
succinyl-Gly-Pro + 7-amino-4-methylcoumarin
succinyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
succinyl-Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Gly-Pro-Leu-Gly-Pro-7-amido-4-methylcoumarin + H2O
succinyl-Gly-Pro-Leu-Gly-Pro + 7-amino-4-methylcoumarin
succinyl-L-Ala-L-Ala-L-Ala-L-Pro-4-nitroanilide + H2O
succinyl-L-Ala-L-Ala-L-Ala-L-Pro + 4-nitroaniline
-
-
-
-
?
succinyl-L-Ala-L-Pro-4-nitroanilide + H2O
succinyl-L-Ala-L-Pro + 4-nitroaniline
-
-
-
-
?
succinyl-L-Arg-L-Pro-4-nitroanilide + H2O
succinyl-L-Arg-L-Pro + 4-nitroaniline
-
-
-
-
?
tasidotin + H2O
tert-butylamine + ?
-
assay at pH 6.8, 37°C
-
-
?
tert-butyloxycarbonyl-Ala-Ala-Pro-Ala p-nitroanilide + H2O
tert-butyloxycarbonyl-Ala-Ala-Pro + Ala + p-nitoaniline
-
-
-
?
thymosin beta4 + H2O
acetyl-N-Ser-Asp-Lys-Pro + ?
-
prolyl oligopeptidase is a second-step enzyme in the release of acetyl-N-Ser-Asp-Lys-Pro from thymosin beta4 and has autoregulatory effect in the first step
-
-
?
Tyr-Gln-Glu-Pro-Val-Leu-Gly-Pro-Val-Arg-Gly-Pro-Phe-Pro-Ile-Ile-Val-p-nitroanilide + H2O
?
urotensin II + H2O
?
-
human substrate, cleavage at the canonical post-proline site
-
-
?
Z-Ala-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Ala-Pro + 7-amino-4-carbamoylmethylcoumarin
Z-Arg-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Arg-Pro + 7-amino-4-carbamoylmethylcoumarin
Z-Asn-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Asn-Pro + 7-amino-4-carbamoylmethylcoumarin
Z-Asp-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Asp-Pro + 7-amino-4-carbamoylmethylcoumarin
Z-Gln-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Gln-Pro + 7-amino-4-carbamoylmethylcoumarin
Z-Glu-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Glu-Pro + 7-amino-4-carbamoylmethylcoumarin
Z-Gly-Pro-4-nitroanilide + H2O
4-nitroaniline + Z-Gly-Pro
-
pH 7.0, room temperature
-
-
?
Z-Gly-Pro-4-nitroanilide + H2O
Z-glycyl-L-proline + 4-nitroaniline
-
assay at pH 7.0, 30°C
-
-
?
Z-Gly-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Gly-Pro + 7-amino-4-carbamoylmethylcoumarin
Z-His-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-His-Pro + 7-amino-4-carbamoylmethylcoumarin
Z-Ile-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Ile-Pro + 7-amino-4-carbamoylmethylcoumarin
Z-Leu-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Leu-Pro + 7-amino-4-carbamoylmethylcoumarin
Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Lys-Pro + 7-amino-4-carbamoylmethylcoumarin
Z-Met-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Met-Pro + 7-amino-4-carbamoylmethylcoumarin
Z-Phe-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Phe-Pro + 7-amino-4-carbamoylmethylcoumarin
Z-Pro-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Pro-Pro + 7-amino-4-carbamoylmethylcoumarin
Z-Ser-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Ser-Pro + 7-amino-4-carbamoylmethylcoumarin
Z-Thr-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Thr-Pro + 7-amino-4-carbamoylmethylcoumarin
Z-Trp-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Trp-Pro + 7-amino-4-carbamoylmethylcoumarin
Z-Tyr-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Tyr-Pro + 7-amino-4-carbamoylmethylcoumarin
Z-Val-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Val-Pro + 7-amino-4-carbamoylmethylcoumarin
(S)-benzyl 2-(2-(4-hydroxynaphthalen-1-ylcarbamoyl)pyrrolidin-1-yl)-2-oxoethylcarbamate + H2O
?
-
specific substrate, UAMC-00682
-
-
?
(S)-benzyl 2-(2-(4-hydroxynaphthalen-1-ylcarbamoyl)pyrrolidin-1-yl)-2-oxoethylcarbamate + H2O
?
-
specific substrate, UAMC-00682
-
-
?
2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala-NH2 + H2O
2-aminobenzoyl-Gly-Phe-Gly-Pro + Phe-Gly-Phe(NO2)-Ala-NH2
-
-
?
2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala-NH2 + H2O
2-aminobenzoyl-Gly-Phe-Gly-Pro + Phe-Gly-Phe(NO2)-Ala-NH2
-
-
?
2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala-NH2 + H2O
2-aminobenzoyl-Gly-Phe-Gly-Pro + Phe-Gly-Phe(NO2)-Ala-NH2
the enzyme binds no more than six residues, P4-P2' even from a longer substrate
-
?
2-aminobenzoyl-Gly-Pro-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gly-Pro + Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
a fluorescence resonance energy transfer peptide
-
-
?
2-aminobenzoyl-Gly-Pro-Gln-N-(2,4-dinitrophenyl)ethylenediamine + H2O
2-aminobenzoyl-Gly-Pro + Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
the fluorescence resonance energy transfer peptide sequence corresponds to bradykinin from human kininogen
-
-
?
Abz-Ala-Ala-Pro-4-nitrophenylalanine + H2O
Abz-Ala-Ala-Pro + 4-nitrophenylalanine
-
about 10% activity compared to Abz-Lys-Pro-4-nitrophenylalanine
-
-
?
Abz-Ala-Ala-Pro-4-nitrophenylalanine + H2O
Abz-Ala-Ala-Pro + 4-nitrophenylalanine
about 50% activity compared to Abz-Lys-Pro-4-nitrophenylalanine
-
-
?
Abz-Ala-Pro-Ala-4-nitrophenylalanine + H2O
Abz-Ala-Pro + L-Ala-4-nitrophenylalanine
-
about 10% activity compared to Abz-Lys-Pro-4-nitrophenylalanine
-
-
?
Abz-Ala-Pro-Ala-4-nitrophenylalanine + H2O
Abz-Ala-Pro + L-Ala-4-nitrophenylalanine
about 27% activity compared to Abz-Lys-Pro-4-nitrophenylalanine
-
-
?
Abz-Ala-Pro-Gly-4-nitrophenylalanine + H2O
Abz-Ala-Pro + Gly-4-nitrophenylalanine
-
about 20% activity compared to Abz-Lys-Pro-4-nitrophenylalanine
-
-
?
Abz-Ala-Pro-Gly-4-nitrophenylalanine + H2O
Abz-Ala-Pro + Gly-4-nitrophenylalanine
about 40% activity compared to Abz-Lys-Pro-4-nitrophenylalanine
-
-
?
Abz-Gly-Gly-Pro-4-nitrophenylalanine + H2O
Abz-Gly-Gly-Pro + 4-nitrophenylalanine
-
about 2% activity compared to Abz-Lys-Pro-4-nitrophenylalanine
-
-
?
Abz-Gly-Gly-Pro-4-nitrophenylalanine + H2O
Abz-Gly-Gly-Pro + 4-nitrophenylalanine
about 20% activity compared to Abz-Lys-Pro-4-nitrophenylalanine
-
-
?
Abz-Gly-Pro-4-nitrophenylalanine + H2O
Abz-Gly-Pro + 4-nitrophenylalanine
-
about 7% activity compared to Abz-Lys-Pro-4-nitrophenylalanine
-
-
?
Abz-Gly-Pro-4-nitrophenylalanine + H2O
Abz-Gly-Pro + 4-nitrophenylalanine
about 20% activity compared to Abz-Lys-Pro-4-nitrophenylalanine
-
-
?
Abz-Lys-Pro-4-nitrophenylalanine + H2O
Abz-Lys-Pro + 4-nitrophenylalanine
-
100% activity
-
-
?
Abz-Lys-Pro-4-nitrophenylalanine + H2O
Abz-Lys-Pro + 4-nitrophenylalanine
100% activity
-
-
?
Arg-Pro-Lys-His-Pro-Ile-Lys-His-Gln + H2O
Arg-Pro-Lys-His-Pro + Ile-Lys-His-Gln
i.e. alphaS1-casein(1-9), cleavage at Pro5-Ile6
-
?
Arg-Pro-Lys-His-Pro-Ile-Lys-His-Gln + H2O
Arg-Pro-Lys-His-Pro + Ile-Lys-His-Gln
i.e. alphaS1-casein(1-9), cleavage at Pro5-Ile6
-
?
benzyloxycarbonyl-Ala-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Gly-Pro + beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Ala-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Gly-Pro + beta-naphthylamine
Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Ala-Pro-p-nitroanilide + H2O
benzyloxycarbonyl-Ala-Pro + p-nitroaniline
Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Ala-Pro-p-nitroanilide + H2O
benzyloxycarbonyl-Ala-Pro + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-D-Ala-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-D-Ala-Gly-Pro + beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-D-Ala-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-D-Ala-Gly-Pro + beta-naphthylamine
Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Gly-Gly-Pro + p-nitrophenol
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Gly-Gly-Pro + p-nitrophenol
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-L-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-L-Pro + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-L-Pro + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-L-Pro + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-L-Pro + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-L-Pro + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-L-Pro + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-2-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + 2-naphthylamine
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-2-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + 2-naphthylamine
-
-
-
?
benzyloxycarbonyl-Gly-Pro-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Gly-Pro-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Gly-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-Pro + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-Pro + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-Pro + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Ala
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Ala
Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Ala
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + 2-naphthylamine
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + 2-naphthylamine
-
-
?
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + beta-naphthylamine
-
-
-
?
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + beta-naphthylamine
Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + beta-naphthylamine
-
-
?
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + beta-naphthylamine
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu + H2O
benzyloxycarbonyl-Gly-Pro + Leu
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu + H2O
benzyloxycarbonyl-Gly-Pro + Leu
Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu + H2O
benzyloxycarbonyl-Gly-Pro + Leu
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Ala
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Ala
Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Ala
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-Leu-D-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Leu-D-Ala
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu-D-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Leu-D-Ala
Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu-D-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Leu-D-Ala
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Gly
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Gly
Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Gly
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Gly-Ala
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Gly-Ala
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Gly + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Gly-Gly
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Gly + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Gly-Gly
-
enzyme from kidney
-
?
Benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro + H2O
Benzyloxycarbonyl-Gly-Pro + Leu-Gly-Pro
Lyophyllum cinerascens
-
-
-
?
Benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro + H2O
Benzyloxycarbonyl-Gly-Pro + Leu-Gly-Pro
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-p-nitroanilide + H2O
benzyloxycarbonyl-Gly-Pro + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-Gly-Pro-p-nitroanilide + H2O
benzyloxycarbonyl-Gly-Pro + p-nitroaniline
Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Gly-Pro-p-nitroanilide + H2O
benzyloxycarbonyl-Gly-Pro + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-Gly-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Gly-Pro + p-nitrophenol
-
-
-
?
benzyloxycarbonyl-Gly-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Gly-Pro + p-nitrophenol
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Gly-Pro + p-nitrophenol
-
-
?
benzyloxycarbonyl-Gly-Pro-Phe + H2O
benzyloxycarbonyl-Gly-Pro + Phe
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Phe + H2O
benzyloxycarbonyl-Gly-Pro + Phe
Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Phe + H2O
benzyloxycarbonyl-Gly-Pro + Phe
-
enzyme from kidney
-
?
benzyloxycarbonyl-glycyl-proline-p-nitroanilide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-glycyl-proline-p-nitroanilide + H2O
?
-
-
-
?
benzyloxycarbonyl-glycyl-proline-p-nitroanilide + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
the pathogen POP degrades host collagen and fibronectin, facilitating cell invasion, selective inhibitors for trypanosome POP block parasite entry into cells
-
-
?
Fibronectin + H2O
?
-
the pathogen POP degrades host collagen and fibronectin, facilitating cell invasion, selective inhibitors for trypanosome POP block parasite entry into cells
-
-
?
gamma-hordein + H2O
?
i.e. SQQQFPQPQQPFPQQP
-
-
?
gluten + H2O
?
-
activity in the human host gastrointestinal tract, overview
-
-
?
gluten + H2O
?
-
degradation of gluten in the human host's intestinal tract, i.e. stomach, duodenum, jejunum, and ileum
-
-
?
gluten + H2O
?
-
determination of activity in a dynamic system that closely mimics the human gastrointestinal tract, overview
-
-
?
gluten peptides + H2O
?
-
activity in the human host gastrointestinal tract, overview
-
-
?
gluten peptides + H2O
?
-
degradation of gluten peptides in the human host's intestinal tract, i.e. stomach, duodenum, jejunum, and ileum
-
-
?
gluten peptides + H2O
?
-
determination of activity in a dynamic system that closely mimics the human gastrointestinal tract, overview
-
-
?
Gly-L-Pro-4-nitroanilide + H2O
Gly-L-Pro + 4-nitroaniline
-
-
-
?
L-Ala-L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala-L-Ala-L-Pro + 4-nitroaniline
-
-
-
-
?
L-Ala-L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala-L-Ala-L-Pro + 4-nitroaniline
-
-
-
-
?
L-Lys-L-Pro-7-amido-4-methylcoumarin + H2O
L-Lys-L-Pro + 7-amino-4-methylcoumarin
-
about 5% activity compared to Z-Gly-L-Pro-7-amido-4-methylcoumarin
-
-
?
L-Lys-L-Pro-7-amido-4-methylcoumarin + H2O
L-Lys-L-Pro + 7-amino-4-methylcoumarin
about 3% activity compared to Z-Gly-L-Pro-7-amido-4-methylcoumarin
-
-
?
LVVYPWTQRF + H2O
LVVYP + WTQRF
-
prolyl endopeptidase activity could be the first step of the degradation of LVV-hemorphin-7
-
?
N-benzyloxycarbonyl-Gly-Pro-4-nitrophenyl ester + H2O
N-benzyloxycarbonyl-Gly-Pro + 4-nitrophenol
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-4-nitrophenyl ester + H2O
N-benzyloxycarbonyl-Gly-Pro + 4-nitrophenol
-
-
-
?
N-carbobenzyloxy-Ala-Pro-2-naphthylamide + H2O
N-carbobenzyloxy-Ala-Pro + 2-naphthylamine
-
-
-
-
?
N-carbobenzyloxy-Ala-Pro-2-naphthylamide + H2O
N-carbobenzyloxy-Ala-Pro + 2-naphthylamine
-
-
-
-
?
N-carbobenzyloxy-Ala-Pro-2-naphthylamide + H2O
N-carbobenzyloxy-Ala-Pro + 2-naphthylamine
-
-
-
-
?
N-succinyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
N-succinyl-Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
N-succinyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
N-succinyl-Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
N-succinyl-glycyl-proline-4-methylcoumarin-7-amide + H2O
N-succinyl-glycyl-proline + 7-amino-4-methylcoumarin
-
-
-
-
?
N-succinyl-glycyl-proline-4-methylcoumarin-7-amide + H2O
N-succinyl-glycyl-proline + 7-amino-4-methylcoumarin
-
-
-
-
?
N-succinyl-glycyl-proline-4-methylcoumarin-7-amide + H2O
N-succinyl-glycyl-proline + 7-amino-4-methylcoumarin
-
-
-
-
?
N-succinyl-glycyl-prolyl-7-amido-4-methylcoumarin + H2O
N-succinyl-glycyl-prolyl + 7-amino-4-methylcoumarin
-
-
-
-
?
N-succinyl-glycyl-prolyl-7-amido-4-methylcoumarin + H2O
N-succinyl-glycyl-prolyl + 7-amino-4-methylcoumarin
-
-
-
-
?
Peptides + H2O
?
-
involved in process of fertilization, between chorion elevation and cell cleavage
-
-
?
Peptides + H2O
?
-
metabolism of peptides containing altered aspartyl residues
-
-
?
Substance P + H2O
?
-
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2
-
-
?
Substance P + H2O
?
-
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2
-
-
?
succinyl-Ala-Pro-4-nitrophenyl ester + H2O
succinyl-Ala-Pro + 4-nitrophenol
-
-
-
?
succinyl-Ala-Pro-4-nitrophenyl ester + H2O
succinyl-Ala-Pro + 4-nitrophenol
-
-
-
?
succinyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
succinyl-Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
succinyl-Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Gly-Pro-4-methylcoumaryl-7-amide + H2O
succinyl-Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
succinyl-Gly-Pro-4-methylcoumaryl-7-amide + H2O
succinyl-Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
succinyl-Gly-Pro-4-methylcoumaryl-7-amide + H2O
succinyl-Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
succinyl-Gly-Pro-4-methylcoumaryl-7-amide + H2O
succinyl-Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
succinyl-Gly-Pro-Leu-Gly-Pro-7-amido-4-methylcoumarin + H2O
succinyl-Gly-Pro-Leu-Gly-Pro + 7-amino-4-methylcoumarin
-
about 58% activity compared to Z-Gly-L-Pro-7-amido-4-methylcoumarin
-
-
?
succinyl-Gly-Pro-Leu-Gly-Pro-7-amido-4-methylcoumarin + H2O
succinyl-Gly-Pro-Leu-Gly-Pro + 7-amino-4-methylcoumarin
about 65% activity compared to Z-Gly-L-Pro-7-amido-4-methylcoumarin
-
-
?
Tyr-Gln-Glu-Pro-Val-Leu-Gly-Pro-Val-Arg-Gly-Pro-Phe-Pro-Ile-Ile-Val-p-nitroanilide + H2O
?
i.e. N-acetyl-beta-casein-(f203-209)-p-nitroanilide, cleavage at: Pro196-Val197, Pro200-Val201 and Pro206-Ile207
-
?
Tyr-Gln-Glu-Pro-Val-Leu-Gly-Pro-Val-Arg-Gly-Pro-Phe-Pro-Ile-Ile-Val-p-nitroanilide + H2O
?
i.e. N-acetyl-beta-casein-(f203-209)-p-nitroanilide, cleavage at: Pro196-Val197, Pro200-Val201 and Pro206-Ile207
-
?
Z-Ala-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Ala-Pro + 7-amino-4-carbamoylmethylcoumarin
-
about 90% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Ala-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Ala-Pro + 7-amino-4-carbamoylmethylcoumarin
about 60% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Arg-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Arg-Pro + 7-amino-4-carbamoylmethylcoumarin
-
about 87% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Arg-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Arg-Pro + 7-amino-4-carbamoylmethylcoumarin
about 90% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Asn-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Asn-Pro + 7-amino-4-carbamoylmethylcoumarin
-
about 30% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Asn-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Asn-Pro + 7-amino-4-carbamoylmethylcoumarin
about 40% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Asp-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Asp-Pro + 7-amino-4-carbamoylmethylcoumarin
-
about 5% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Asp-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Asp-Pro + 7-amino-4-carbamoylmethylcoumarin
about 10% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Gln-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Gln-Pro + 7-amino-4-carbamoylmethylcoumarin
-
about 38% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Gln-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Gln-Pro + 7-amino-4-carbamoylmethylcoumarin
about 38% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Glu-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Glu-Pro + 7-amino-4-carbamoylmethylcoumarin
-
about 18% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Glu-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Glu-Pro + 7-amino-4-carbamoylmethylcoumarin
about 20% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Gly-L-Pro-4-nitroanilide + H2O
Z-Gly-L-Pro + 4-nitroaniline
-
-
-
-
?
Z-Gly-L-Pro-4-nitroanilide + H2O
Z-Gly-L-Pro + 4-nitroaniline
-
-
-
-
?
Z-Gly-L-Pro-4-nitroanilide + H2O
Z-Gly-L-Pro + 4-nitroaniline
-
highest activity
-
-
?
Z-Gly-L-Pro-4-nitroanilide + H2O
Z-Gly-L-Pro + 4-nitroaniline
-
highest activity
-
-
?
Z-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
Z-Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
Z-Gly-L-Pro + 7-amino-4-methylcoumarin
100% activity
-
-
?
Z-Gly-Pro-4-nitroanilide + H2O
Z-Gly-Pro + p-nitroaniline
assay at pH 8.0, 34°C
-
-
?
Z-Gly-Pro-4-nitroanilide + H2O
Z-Gly-Pro + p-nitroaniline
assay at pH 5.0, 37°C
-
-
?
Z-Gly-Pro-4-nitroanilide + H2O
Z-Gly-Pro + p-nitroaniline
assay at 37°C
-
-
?
Z-Gly-Pro-4-nitroanilide + H2O
Z-Gly-Pro + p-nitroaniline
-
chromogenic assay, assay at pH 7.0, 37°C, reaction stopped by addition of sodium acetate
-
-
?
Z-Gly-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Gly-Pro + 7-amino-4-carbamoylmethylcoumarin
-
about 22% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Gly-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Gly-Pro + 7-amino-4-carbamoylmethylcoumarin
about 70% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Gly-Pro-7-amido-4-methylcoumarin
Z-Gly-Pro + 7-amino-4-methylcoumarin
-
fluorogenic assay, assay at pH 6.8, 37°C, reaction stopped by addition of acetic acid
-
-
?
Z-Gly-Pro-7-amido-4-methylcoumarin
Z-Gly-Pro + 7-amino-4-methylcoumarin
-
assay at pH 8.0, 37°C, reaction stopped with sodium acetate
-
-
?
Z-Gly-Pro-7-amido-4-methylcoumarin
Z-Gly-Pro + 7-amino-4-methylcoumarin
-
assay at pH 7.0, 30°C
-
-
?
Z-Gly-Pro-7-amido-4-methylcoumarin + H2O
z-Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Gly-Pro-7-amido-4-methylcoumarin + H2O
z-Gly-Pro + 7-amino-4-methylcoumarin
-
assay at pH 7.0, 30°C
-
-
?
Z-Gly-Pro-7-amido-4-methylcoumarin + H2O
z-Gly-Pro + 7-amino-4-methylcoumarin
-
assay at pH 7.0, 37°C
-
-
?
Z-His-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-His-Pro + 7-amino-4-carbamoylmethylcoumarin
-
about 58% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-His-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-His-Pro + 7-amino-4-carbamoylmethylcoumarin
about 65% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Ile-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Ile-Pro + 7-amino-4-carbamoylmethylcoumarin
-
about 92% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Ile-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Ile-Pro + 7-amino-4-carbamoylmethylcoumarin
about 60% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-L-Ala-L-Ala-L-Ala-L-Pro-4-nitroanilide + H2O
Z-L-Ala-L-Ala-L-Ala-L-Pro + 4-nitroaniline
-
-
-
-
?
Z-L-Ala-L-Ala-L-Ala-L-Pro-4-nitroanilide + H2O
Z-L-Ala-L-Ala-L-Ala-L-Pro + 4-nitroaniline
-
-
-
-
?
Z-Leu-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Leu-Pro + 7-amino-4-carbamoylmethylcoumarin
-
about 70% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Leu-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Leu-Pro + 7-amino-4-carbamoylmethylcoumarin
about 50% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Lys-Pro + 7-amino-4-carbamoylmethylcoumarin
-
100% activity
-
-
?
Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Lys-Pro + 7-amino-4-carbamoylmethylcoumarin
100% activity
-
-
?
Z-Met-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Met-Pro + 7-amino-4-carbamoylmethylcoumarin
-
about 68% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Met-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Met-Pro + 7-amino-4-carbamoylmethylcoumarin
about 67% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Phe-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Phe-Pro + 7-amino-4-carbamoylmethylcoumarin
-
about 48% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Phe-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Phe-Pro + 7-amino-4-carbamoylmethylcoumarin
about 65% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Pro-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Pro-Pro + 7-amino-4-carbamoylmethylcoumarin
-
about 3% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Pro-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Pro-Pro + 7-amino-4-carbamoylmethylcoumarin
about 3% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Ser-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Ser-Pro + 7-amino-4-carbamoylmethylcoumarin
-
about 30% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Ser-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Ser-Pro + 7-amino-4-carbamoylmethylcoumarin
about 60% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Thr-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Thr-Pro + 7-amino-4-carbamoylmethylcoumarin
-
about 75% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Thr-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Thr-Pro + 7-amino-4-carbamoylmethylcoumarin
about 50% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Trp-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Trp-Pro + 7-amino-4-carbamoylmethylcoumarin
-
about 23% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Trp-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Trp-Pro + 7-amino-4-carbamoylmethylcoumarin
about 30% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Tyr-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Tyr-Pro + 7-amino-4-carbamoylmethylcoumarin
-
about 60% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Tyr-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Tyr-Pro + 7-amino-4-carbamoylmethylcoumarin
about 70% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Val-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Val-Pro + 7-amino-4-carbamoylmethylcoumarin
-
about 20% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
Z-Val-Pro-7-amido-4-carbamoylmethylcoumarin + H2O
Z-Val-Pro + 7-amino-4-carbamoylmethylcoumarin
about 38% activity compared to Z-Lys-Pro-7-amido-4-carbamoylmethylcoumarin
-
-
?
additional information
?
-
-
leginsulin appears to be a possible candidate for the POP substrate
-
-
?
additional information
?
-
-
no activity with L-Ala-L-Pro-4-nitroanilide and L-Ala-L-Pro-L-Phe-4-nitroanilide
-
-
?
additional information
?
-
-
no activity toward L-Pro-4-nitroanilide, Gly-L-Pro-4-nitroanilide, Z-Pro-nitrophenyl ester, Z-Gly-Gly-nitrophenyl ester, Z-Phe-Arg-7-amido-4-methylcoumarin, Z-Leu-Leu-Glu-7-amido-4-methylcoumarin, Z-Val-Lys-Met-7-amido-4-methylcoumarin, Z-Leu-Leu-Leu-7-amido-4-methylcoumarin, and Z-Tyr-Val-Ala-Asp-4-nitroanilide
-
-
?
additional information
?
-
-
cellular functions, overview, POP may regulate phosphoinositide signaling, overview
-
-
?
additional information
?
-
-
enzyme inhibition leads to inhibition of lithium effects, the loss of enzyme activity evokes a 4fold increase in the inositol-3-phosphate concentration counteracting the Li+ ions, enzyme regulation, overview
-
-
?
additional information
?
-
-
substrate specificity with exclusion of peptides with more than 30 amino acids, overview
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, substrate specificity, overview
-
-
?
additional information
?
-
-
requirement for a trans peptide bond immediately preceding the active bond
-
-
?
additional information
?
-
-
not: (7-D-Pro)oxytocin and high molecular weight proteins even after denaturation
-
-
?
additional information
?
-
-
no hydrolysis of Pro-beta-naphthylamide, benzyloxycarbonyl-Pro-beta-naphthylamide, benzyloxycarbonyl-Ala-p-nitrophenol, Gly-Prp-beta-naphthylamide, Ala-Ala-beta-naphthylamide, benzyloxycarbonyl-Gly-Pro-D-Ala
-
?
additional information
?
-
-
the enzyme plays a role in the metabolism of proline-containing neuropeptides which have been suggested to be involved in learning and memory processes
-
?
additional information
?
-
-
cellular functions, overview
-
-
?
additional information
?
-
-
the enzyme induces cleavage of gluten-derived peptides predigested by pepsin and pancreatic enzymes an exhibiting a detoxifying effect in the host's gut
-
-
?
additional information
?
-
-
the enzyme is a proline-specific endopeptidase with a serine-type mechanism
-
-
?
additional information
?
-
-
substrate specificity with exclusion of peptides with more than 30 amino acids, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, the S2' subsite had the highest specificity of the S1'-S3' subsites, this subsite prefers Pro residues, followed by Leu, Met, Phe, and Ala residues, the S1' subsite has lower specificity than the S2', with the strongest preference for hydrophobic, e.g. Leu, and aromatic, e.g. Phe, residues, and the greatest discrimination against Pro residues
-
-
?
additional information
?
-
-
the enzyme removes most of the gut-digestion-resistant gliadin peptides in the host gut luman of coeliac disease patients, overview, enzyme regulation, overview
-
-
?
additional information
?
-
-
the enzyme cleaves at the C-terminal side of proline residues, the bacterial enzyme is also capable of cleaving Ala-Xaa and Val-Xaa bonds, no activity with large proteins with over 30 amino acids
-
-
?
additional information
?
-
-
no activity with Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2, pGlu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr and pGly-His-Trp-Ser-tyr-Gly-leu-Arg-Pro-Gly-NH2
-
?
additional information
?
-
splice variant PRPL A, no cleavage of peptide substrates containing a P1 basic residue, very slow reaction with activated ester substrate 4-methylumbelliferyl-p-guanidinobenzoate
-
-
?
additional information
?
-
-
cellular functions, overview, POP may regulate phosphoinositide signaling, overview, the enzyme is involved in neuronal degeneration and Alzheimer's disease with enzyme inhibition leading to a reduction of beta-amyloid peptide, overview
-
-
?
additional information
?
-
-
POP activity levels are lowered in different stages of depression, whereas activity is increased in patients with mania and schizophrenia, the antidepressant fluoxetine and the antimanic drug valproic acid both restore POP activity to normal levels
-
-
?
additional information
?
-
-
the enzyme is a serine protease, that digests small peptide-like hormones, neuroactive peptides, and various cellular factors, it is implicated in several biological processes and diseases, e.g. in some psychiatric disorders, most probably through interference in the inositol cycle, it is important in the metabolism of substance P, arginine vasopressin, thyroliberin, and gonadoliberin, enzyme regulation probably involving gluten, prep expression is downregulated in coelic disease patients in complete remission, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the phosphoinositide pathway, in formation and processing of amyloid beta-peptide, protein secretion, and in neuronal differentiation and maturation, overview, the enzyme is involved in several diseases, e.g. celiac disease, Alzheimer's diease, Parkinsons's disease, affective disorders, eating disorders, cancer, inflammation, hypertension, and neurodegenarative disorders, overview, enzyme inhibition positively affects neurodiseases, overview
-
-
?
additional information
?
-
-
the enzyme is involved with the inactivation of regulatory neuropeptides, enzyme activity is correlated to an increase in protein secretion, suggesting that the enzyme may be involved in regulating secretory processes
-
-
?
additional information
?
-
-
the enzyme plays a role in inositol 1,4,5-triphosphate signaling and in the actions of antidepressants, POP inhibitors have antiamnesic and neuroprotective properties, overview
-
-
?
additional information
?
-
-
no activity with gluten in celiac sprue patients, substrate specificity with exclusion of peptides with more than 30 amino acids, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, the enzyme cleaves at the C-terminal side of proline residues and more slowly of alanine residues, no activity with large proteins with over 30 amino acids
-
-
?
additional information
?
-
-
the enzyme cleaves the peptide bond on the C-terminal side of proline in peptides up to approx 30 residues, and hydrolyse several peptide hormones and neuropeptides in vitro
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme shows endopeptidase activity with peptides no longer than 30 amino acids
-
-
?
additional information
?
-
-
cleaves short proline-containing neuropeptides, and is involved in memory and learning
-
-
?
additional information
?
-
-
fibroblast activation protein prefers uncharged residues, including small or bulky hydrophobic amino acids, but not charged amino acids, especially acidic residue at P1, P3 and P4 sites. Fibroblast activation protein cannot cleave interleukins
-
-
?
additional information
?
-
-
prolyl oligopeptidase colocalizes with alpha-synuclein, beta-amyloid, tau protein and astroglia in the post-mortem brain samples with Parkinsons and Alzheimers diseases
-
-
?
additional information
?
-
-
no activity with Abz-L-Pro-L-Pro-4-nitrophenylalanine, Abz-L-Pro-L-Pro-L-Ala-4-nitrophenylalanine, Gly-L-Pro-7-amido-4-methylcoumarin, and L-Pro-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
the specificity for post-proline bonds suggests that the enzyme may play a central role in the hydrolysis of casein-derived bitter peptides, such as beta-casein(f193-209)
-
?
additional information
?
-
-
the specificity for post-proline bonds suggests that the enzyme may play a central role in the hydrolysis of casein-derived bitter peptides, such as beta-casein(f193-209)
-
?
additional information
?
-
the specificity for post-proline bonds suggests that the enzyme may play a central role in the hydrolysis of casein-derived bitter peptides, such as beta-casein(f193-209)
-
?
additional information
?
-
-
the specificity for post-proline bonds suggests that the enzyme may play a central role in the hydrolysis of casein-derived bitter peptides, such as beta-casein(f193-209)
-
?
additional information
?
-
-
leginsulin appears to be a possible candidate for the POP substrate
-
-
?
additional information
?
-
Lyophyllum cinerascens
-
no hydrolysis of Pro-beta-naphthylamide, benzyloxycarbonyl-Pro-beta-naphthylamide, Gly-Pro-beta-naphthylamide, benzyloxycarbonyl-Gly-D-Pro-p-nitroanilide, benzyloxycarbonyl-D-Ala-Pro-beta-naphthylamide and benzyloxycarbonyl-Gly-Pro-D-Ala
-
?
additional information
?
-
-
cellular functions, overview, POP may regulate phosphoinositide signaling, overview, the enzyme is involved in Alzheimer's disease with enzyme inhibition leading to a reduction of beta-amyloid peptide, overview
-
-
?
additional information
?
-
-
the enzyme is a serine protease, that digests small peptide-like hormones, neuroactive peptides, and various cellular factors, it is implicated in several biological processes and diseases, e.g. in some psychiatric disorders, most probably through interference in the inositol cycle, it is important in the metabolism of substance P, arginine vasopressin, thyroliberin, and gonadoliberin, enzyme regulation, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the phosphoinositide pathway, in formation and processing of amyloid beta-peptide, protein secretion, and in neuronal differentiation and maturation, overview, the enzyme is involved in several diseases, e.g. celiac disease, Alzheimer's diease, Parkinsons's disease, affective disorders, eating disorders, cancer, inflammation, hypertension, and neurodegenarative disorders, overview, enzyme inhibition can improve the retention time when administered before either the acquisition or the retential trial in scopolamine-induced amnesia, enzyme inhibition positively affects neurodiseases, overview
-
-
?
additional information
?
-
-
substrate specificity with exclusion of peptides with more than 30 amino acids, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, the enzyme cleaves at the C-terminal side of proline residues and more slowly of alanine residues, no activity with large proteins with over 30 amino acids
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme shows endopeptidase activity with peptides no longer than 3 amino acids
-
-
?
additional information
?
-
-
substrate specificity with exclusion of peptides with more than 30 amino acids, overview
-
-
?
additional information
?
-
-
the enzyme cleaves the peptide bond on the C-terminal side of proline in peptides up to approx 30 residues, substrate entry into the active site cavity, substrate-binding structure and mechanism, overview
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, substrate specificity, overview
-
-
?
additional information
?
-
-
no activity with Ala-Pro-4-nitroanilide, Arg-Pro-4-nitroanilide, Val-Ala-4-nitroanilide, Gly-Pro-4-nitroanilide, Leu-4-nitroanilide, Pro-4-nitroanilide, Glu-4-nitroanilide, and Glu-Ala-4-nitroanilide
-
-
?
additional information
?
-
-
no activity with Ala-Pro-4-nitroanilide, Arg-Pro-4-nitroanilide, Val-Ala-4-nitroanilide, Gly-Pro-4-nitroanilide, Leu-4-nitroanilide, Pro-4-nitroanilide, Glu-4-nitroanilide, and Glu-Ala-4-nitroanilide
-
-
?
additional information
?
-
-
substrate specificity with exclusion of peptides with more than 30 amino acids, overview
-
-
?
additional information
?
-
-
the enzyme cleaves at the C-terminal side of proline residues, the bacterial enzyme is also capable of cleaving Ala-Xaa and Val-Xaa bonds, no activity with large proteins with over 30 amino acids
-
-
?
additional information
?
-
the enzyme cleaves the peptide bond on the C-terminal side of proline in peptides up to approx 30 residues, substrate entry into the active site cavity, substrate-binding structure and mechanism, the loops connecting the peptidase and propeller domains act like a hinge, holding the structure together as the domains move apart, creating a large opening, overview
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, substrate specificity, overview
-
-
?
additional information
?
-
ability to cleave immunotoxic gluten peptides endoproteolytically, attractive oral therapeutic candidates for protecting celiac sprue patients from the toxic effects of dietary gluten
-
-
?
additional information
?
-
-
no hydrolysis of benzyloxycarbonyl-D-Pro-p-nitrophenol, negligibly small hydrolysis rate with benzyloxycarbonyl-D-Ala-Pro-p-nitrophenol
-
?
additional information
?
-
-
cellular functions, overview, POP may regulate phosphoinositide signaling, overview
-
-
?
additional information
?
-
-
substrate specificity with exclusion of peptides with more than 30 amino acids, overview
-
-
?
additional information
?
-
-
substrate specificity with exclusion of peptides with more than 30 amino acids, overview
-
-
?
additional information
?
-
-
the enzyme cleaves the peptide bond on the C-terminal side of proline in peptides up to approx 30 residues, substrate entry into the active site cavity, substrate-binding structure and mechanism, general acid/base catalysis is the rate-limiting step, overview
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, substrate specificity, overview
-
-
?
additional information
?
-
-
tissue-dependent peptide hydrolysis evoked by prolyl endopeptidase activity is involved in the water-electrolyte homeostasis
-
?
additional information
?
-
-
cellular functions, overview, POP may regulate phosphoinositide signaling, overview
-
-
?
additional information
?
-
-
the enzyme in the brain dopaminergix system is involved in the pathogenesis of doamine deficiency-dependent depressive states, and is activated in association with development of MPTP-induced depressive syndrome in the brain frontal cortex, overview
-
-
?
additional information
?
-
-
the enzyme is a serine protease, that digests small peptide-like hormones, neuroactive peptides, and various cellular factors, it is implicated in several biological processes and diseases, e.g. in some psychiatric disorders, most probably through interference in the inositol cycle, it is important in the metabolism of substance P, arginine vasopressin, thyroliberin, and gonadoliberin, enzyme regulation, overview
-
-
?
additional information
?
-
-
the enzyme is associated with cognitive functions and inositol 1,4,5-triphosphate signaling, and plays a role in modifying neuropeptide levels, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the phosphoinositide pathway, in formation and processing of amyloid beta-peptide, protein secretion, and in neuronal differentiation and maturation, overview, the enzyme is involved in several diseases, e.g. celiac disease, Alzheimer's diease, Parkinsons's disease, affective disorders, eating disorders, cancer, inflammation, hypertension, and neurodegenarative disorders, overview, enzyme inhibition can improve the retention time when administered before either the acquisition or the retential trial in scopolamine-induced amnesia, enzyme inhibition also positively affects neurodiseases, overview
-
-
?
additional information
?
-
-
the enzyme is involved with the inactivation of regulatory neuropeptides
-
-
?
additional information
?
-
-
the enzyme plays a role in inositol 1,4,5-triphosphate signaling and in the actions of antidepressants, POP inhibitors have antiamnesic and neuroprotective properties, overview
-
-
?
additional information
?
-
-
no activity with gluten in celiac sprue rats, substrate specificity with exclusion of peptides with more than 30 amino acids, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, the enzyme cleaves at the C-terminal side of proline residues and more slowly of alanine residues, no activity with large proteins with over 30 amino acids
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme shows endopeptidase activity with peptides no longer than 3 amino acids
-
-
?
additional information
?
-
-
the serine protease cleaves at the C-terminal side of proline residues and more slowly of alanine residues of peptides with no more than 30 amino acids
-
-
?
additional information
?
-
-
hydrolyzes proline-containing peptides shorter than 30 amino acids
-
-
?
additional information
?
-
-
is involved in thalamocortical and corticothalamic signal processing
-
-
?
additional information
?
-
prolyl oligopeptidase binds to the growth-38 associated protein GAP-43, which is a key regulator of synaptic plasticity
-
-
?
additional information
?
-
-
the recombinant prolyl oligopeptidase is not able to cleave whole 43-mer thymosin beta4, while it is effective at hydrolyzing somatostatin-28 (1-12)
-
-
?
additional information
?
-
no activity with Abz-L-Pro-L-Pro-4-nitrophenylalanine, Abz-L-Pro-L-Pro-L-Ala-4-nitrophenylalanine, Gly-L-Pro-7-amido-4-methylcoumarin, and L-Pro-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
-
no activity with Abz-L-Pro-L-Pro-4-nitrophenylalanine, Abz-L-Pro-L-Pro-L-Ala-4-nitrophenylalanine, Gly-L-Pro-7-amido-4-methylcoumarin, and L-Pro-7-amido-4-methylcoumarin
-
-
?
additional information
?
-
no activity with human hemoglobin, human serum albumin, human collagen type I, and human collagen type IV
-
-
?
additional information
?
-
-
no activity with human hemoglobin, human serum albumin, human collagen type I, and human collagen type IV
-
-
?
additional information
?
-
-
cellular functions, overview, POP may regulate phosphoinositide signaling, overview
-
-
?
additional information
?
-
the enzyme is a serine protease, that digests small peptide-like hormones, neuroactive peptides, and various cellular factors, it is implicated in several biological processes and diseases, e.g. in some psychiatric disorders, most probably through interference in the inositol cycle, it is important in the metabolism of substance P, arginine vasopressin, thyroliberin, and gonadoliberin, enzyme regulation, overview
-
-
?
additional information
?
-
-
no activity with gluten in celiac sprue patients, substrate specificity with exclusion of peptides with more than 30 amino acids, overview
-
-
?
additional information
?
-
-
POP is a proline-specific peptidase that hydrolyzes oligopeptides after prolyl residues, the S1 binding site of POP has evolved to fit the pyrrolidine ring of an L-prolyl residue
-
-
?
additional information
?
-
substrate specificity, overview, the enzyme cleaves at the C-terminal side of proline residues and more slowly of alanine residues, no activity with large proteins with over 30 amino acids
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, substrate specificity, overview
-
-
?
additional information
?
-
-
substance P, arginine-vasopressin, thyroliberin and gonadoliberin are proposed physiological substrates of this protease. No ZPP-sensitive cleavage occurred with the 33-mer, PEP-3, PEP-26, PEP-48_2, and PEP-50
-
-
?
additional information
?
-
substrates require a proline in position P1, with the exception of N-succinyl-L-Ala-L-Ala-L-Ala-7-amino-4-methylcoumarin
-
-
?
additional information
?
-
-
substrates require a proline in position P1, with the exception of N-succinyl-L-Ala-L-Ala-L-Ala-7-amino-4-methylcoumarin
-
-
?
additional information
?
-
-
enzyme inhibitors are able to prevent the in vitro invasion of rodent muscle cells by trypomastigotes
-
-
?
additional information
?
-
-
the enzyme cleaves the peptide bond on the C-terminal side of proline in peptides up to approx 30 residues, substrate entry into the active site cavity, substrate-binding structure and mechanism, overview
-
-
?
additional information
?
-
-
specifically hydrolyzes Pro-Xaa bonds, exerts a low specificity towards residues in position P1', except for Glu and P2 and does not cleave the proline bonds in long substrates such as ribonuclease
-
?
