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Information on EC 3.4.21.26 - prolyl oligopeptidase and Organism(s) Sus scrofa and UniProt Accession P23687
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3.4.21.26 prolyl oligopeptidaseSpecify your search results
Word Map
- 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
The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
prolyl oligopeptidase, fibroblast activation protein, proline endopeptidase, post-proline cleaving enzyme, prolylendopeptidase, proline-specific endopeptidase, post-proline endopeptidase, glutenase, prolyl endoprotease, pepo2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
endoprolylpeptidase
-
-
-
-
peptidase, postproline endo-
-
-
-
-
post-proline cleaving enzyme
-
-
-
-
post-proline endopeptidase
-
-
-
-
postproline endopeptidase
-
-
-
-
postproline-cleaving enzyme
-
-
-
-
proline endopeptidase
-
-
-
-
proline-specific endopeptidase
-
-
-
-
prolyl endopeptidase
additional information
-
the enzyme is a member of the serine peptidase family with post-proline cleaving activity towards peptides
prolyl endopeptidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic mechanism, structure-function relationship
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
the catalytic triad Ser554, Asp641, His680 is located at the C-terminus in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance, catalytic mechanism, structure-function relationship, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY
72162-84-6
-
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
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-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
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-p-nitrophenol + H2O
benzyloxycarbonyl-Gly-Pro + p-nitrophenol
-
-
?
benzyloxycarbonyl-Gly-Pro-SBzl + H2O
benzyloxycarbonyl-Gly-Pro + phenyl-methanethiol
-
-
?
N-benzyloxycarbonyl-Gly-Pro-4-nitrophenyl ester + H2O
N-benzyloxycarbonyl-Gly-Pro + 4-nitrophenol
-
-
-
?
succinyl-Ala-Pro-4-nitrophenyl ester + H2O
succinyl-Ala-Pro + 4-nitrophenol
-
-
-
?
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-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
-
-
?
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
-
-
?
alpha-synulein + H2O
?
-
the enzyme binds to alpha-synuclein and enhances its dimerization
-
-
?
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
-
-
?
N-succinyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
N-succinyl-Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
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
-
-
?
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
Z-Gly-Pro-7-amido-4-methylcoumarin
Z-Gly-Pro + 7-amino-4-methylcoumarin
-
assay at pH 7.0, 30°C
-
-
?
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
-
?
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + beta-naphthylamine
-
-
?
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + beta-naphthylamine
-
-
?
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
-
-
?
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
-
-
-
?
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
?
-
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
?
-
-
cellular functions, overview, POP may regulate phosphoinositide signaling, 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
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL 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
alpha-synulein + H2O
?
-
the enzyme binds to alpha-synuclein and enhances its dimerization
-
-
?
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
?
-
-
cellular functions, overview, POP may regulate phosphoinositide signaling, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no significant differences between membrane PE and POP regarding the sensitivity to the metals
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R)-1-(1-[[3-(azepan-1-ylcarbonyl)phenyl]carbonyl]-L-prolyl)pyrrolidine-2-carbonitrile
50% inhibition at 4.6 nM
(2R)-1-(1-[[4-(pyrrolidin-1-ylcarbonyl)phenyl]carbonyl]-L-prolyl)pyrrolidine-2-carbonitrile
50% inhibition at 1.6 nM
(2R)-1-[1-(4-azepan-1-yl-4-oxobutanoyl)-L-prolyl]pyrrolidine-2-carbonitrile
50% inhibition at 0.76 nM
(2R)-1-[1-(4-oxo-4-pyrrolidin-1-ylbutanoyl)-L-prolyl]pyrrolidine-2-carbonitrile
50% inhibition at 2.9 nM
(2R)-1-[1-(5-azepan-1-yl-3,3-dimethyl-5-oxopentanoyl)-L-prolyl]pyrrolidine-2-carbonitrile
50% inhibition at 0.39 nM
(2R)-1-[1-(5-azepan-1-yl-5-oxopentanoyl)-L-prolyl]pyrrolidine-2-carbonitrile
50% inhibition at 1.2 nM
(2S)-1-[1-(3-[[(2S)-2-(cyclopentylcarbonyl)pyrrolidin-1-yl]carbonyl]benzoyl)-L-prolyl]pyrrolidine-2-carbonitrile
-
(2S)-1-[[(2S)-1-(1-oxo-4-phenylbutyl)-2-pyrrolidinyl]carbonyl]-2-pyrrolidinecarbonitrile
i.e. KYP-2047
1-(3-oxo-3-[(2S)-2-(pyrrolidinocarbonyl)pyrrolidin-1-yl]propyl)-3-phenylquinoxalin-2(1H)-one
-
1-(4-oxo-4-[(2S)-2-(pyrrolidinocarbonyl)pyrrolidin-1-yl]butyl)-3-phenylquinoxalin-2(1H)-one
-
1-[(2R,5S)-2-(propan-2-yl)-5-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]-4-(pyridin-3-yl)butan-1-one
-
1-[(2R,5S)-2-tert-butyl-5-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]-4-phenylbutan-1-one
-
2-(3-[(2S)-4,4-difluoro-2-(pyrrolidinocarbonyl)pyrrolidin-1-yl]-3-oxopropyl) isoindole-1,3(2H)-dione
-
2-(4-oxo-4-[(2S)-2-(pyrrolidinocarbonyl)pyrrolidin-1-yl]butyl)-1H-isoindole-1,3(2H)-dione
-
2-[3-oxo-3-[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]propyl]-1H-isoindole-1,3(2H)-dione
-
3-(3-oxo-3-[(2S)-2-(pyrrolidinocarbonyl)pyrrolidin-1-yl]propyl)-5,5-diphenylimidazolidine-2,4-dione
-
3-(4-oxo-4-[(2S)-2-(pyrrolidinocarbonyl)pyrrolidin-1-yl]butyl)-5,5-diphenylimidazolidine-2,4-dione
-
3-cyclohexyl-N-[(2S)-1-oxo-3-phenyl-1-[(2S)-2-(piperidin-1-ylcarbonyl)pyrrolidin-1-yl]propan-2-yl]propanamide
-
4-phenyl-1-[(2S)-2-[[(2S)-2-(1,3-thiazol-2-ylcarbonyl)pyrrolidin-1-yl]carbonyl]pyrrolidin-1-yl]butan-1-one
-
4-phenylbutanoyl-5(R)-tert-butyl-L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine
-
cyclopent-2-ene-1,2-dicarboxylic acid 2-benzylamide 1-[2(S)-(hydroxyacetyl)-H-pyrrolidine]amide
-
N-[(2S)-3-methyl-1-oxo-1-[(2S)-2-(piperidin-1-ylcarbonyl)pyrrolidin-1-yl]butan-2-yl]-3-phenoxybenzamide
-
(2S)-1-[1-[(3-[[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]carbonyl]phenyl)carbonyl]-D-prolyl]pyrrolidine-2-carbaldehyde
-
functional CHO group is the principal factor determining the inhibition kinetics
(2S)-1-[1-[(3-[[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]carbonyl]phenyl)carbonyl]-L-prolyl]pyrrolidine-2-carbonitrile
-
-
(2S,2'S)-1,1'-(benzene-1,3-diyldicarbonyl)bis[2-(pyrrolidin-1-ylcarbonyl)pyrrolidine]
-
-
2-hydroxy-1-[(2S)-1-[1-[(3-[[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]carbonyl]phenyl)carbonyl]-D-prolyl]pyrrolidin-2-yl]ethanone
-
functional CHO group is the principal factor determining the inhibition kinetics
3-(2(S)-benzoyl-pyrrolidine-1-carbonyl)-benzoyl-5(R)-tert-butyl-L-Pro-pyrrolidine
-
IC50: 460 nM
4-phenylbutanoyl-5(R)-methyl-L-Pro-2(S)-(hydroxyacetyl)pyrrolidine
-
IC50: 0.15 nM
4-phenylbutanoyl-5(R)-tert-butyl-L-Pro-2(S)-(hydroxyacetyl)-pyrrolidine
-
IC50: 0.26 nM
isophthalic acid (L-proline methyl ester) L-prolyl-pyrrolidine amide
-
IC50: 54 nM
isophthalic acid 2(S)-(cyclopentanecarbonyl)pyrrolidine (L-proline methyl ester) amide
-
IC50: 640 nM
isophthalic acid 2(S)-(cyclopentanecarbonyl)pyrrolidine L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine amide
-
IC50: 0.61 nM, log P: 0.2, the log P value is a first prediction of the blood-brain barrier penetrability
isophthalic acid 2(S)-(cyclopentanecarbonyl)pyrrolidine-L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine amide
-
-
isophthalic acid 2(S)-(cyclopentanecarbonyl)pyrrolidine-L-prolyl-2(S)-cyanopyrrolidine amide
-
-
isophthalic acid 2(S)-(cyclopentylcarbonyl)pyrrolidine L-prolyl-pyrrolidine amide
-
IC50: 14 nM, log P: 1.1, the log P value is a first prediction of the blood-brain barrier penetrability
isophthalic acid 2(S)-(cylcohexanecarbonyl)pyrrolidine L-prolyl-2(S)-cynaopyrrolidine amide
-
IC50: 0.72 nM
isophthalic acid 2(S)-(cylcopentanecarbonyl)pyrrolidine L-prolyl-2(S)-cynaopyrrolidine amide
-
IC50: 1.1 nM, log P: 0.8, the log P value is a first prediction of the blood-brain barrier penetrability
isophthalic acid 2(S)-acetylpyrrolidine L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine amide
-
IC50: 1.2 nM
isophthalic acid 2(S)-acetylpyrrolidine L-prolyl-2(S)-cynaopyrrolidine amide
-
IC50: 4.2 nM, log P: -0.6, the log P value is a first prediction of the blood-brain barrier penetrability
isophthalic acid 2(S)-benzoylpyrrolidine L-prolyl-2(S)-cynaopyrrolidine amide
-
IC50: 1.3 nM, log P: 1.1, the log P value is a first prediction of the blood-brain barrier penetrability
isophthalic acid 2(S)-isobutanoylpyrrolidine L-prolyl-2(S)-cynaopyrrolidine amide
-
IC50: 1.6 nM, log P: 0.3, the log P value is a first prediction of the blood-brain barrier penetrability
isophthalic acid bis-2(S)-(cyclopentanecarbonyl)pyrrolidine amide
-
IC50: 78 nM, log P: 2.7, the log P value is a first prediction of the blood-brain barrier penetrability
isophthalic acid L-prolyl-2(S)-cyanopyrrolidine L-prolyl-pyrrolidine amide
-
IC50: 1.5 nM
isophthalic acid L-prolyl-pyrrolidine L-prolyl-L-prolinal amide
-
IC50: 1.3 nM
phenylmethanesulfonyl fluoride
-
PE and POP are partially resistant to phenylmethanesulfonyl fluoride, a generic serine protease inhibitor that has a low efficiency in inhibiting POP
isophthalic acid bis(L-prolyl-pyrrolidine) amide
-
IC50: 26 nM, log O = -0.2, the log P value is a first prediction of the blood-brain barrier penetrability
isophthalic acid L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine L-prolyl-pyrrolidine amide
-
0.00039 nM
isophthalic acid L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine L-prolyl-pyrrolidine amide
-
IC50: 0.39 nM
additional information
structure-function relationship of inhibitors, specificity at the P2 and S3 position, overview
-
additional information
-
specific dipeptidyl peptidase IV inhibitor HIV-1 tat (1-9) fragment with sequence H-Met-Asp-Pro-Val-Asp-Pro-Asn-Ile-Glu-OH
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00205
2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala-NH2
pH 8.0, wild-type enzyme
0.0192
benzyloxycarbonyl-Gly-Pro-p-nitrophenyl ester
pH 7.0, wild-type enzyme
0.00042 - 0.00082
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
0.0009 - 0.00111
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
0.00024
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.00033 - 0.00047
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
0.00084 - 0.00154
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Ile-Gly-GLu-Ile-Lys-Glu-Glu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
0.00141
2-aminobenzoyl-Gly-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.00117
2-aminobenzoyl-Gly-Pro-Phe-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.0019
2-aminobenzoyl-Gly-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.0054
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide
pH 7.0, mutant enzyme D641A
0.0059
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide
pH 7.0, wild-type enzyme
0.0135
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide
pH 7.0, mutant enzyme D641N
0.000025
benzyloxycarbonyl-Gly-Pro-p-nitrophenol
pH 7.0, mutant enzyme D641A
0.000028
benzyloxycarbonyl-Gly-Pro-p-nitrophenol
pH 7.0, mutant enzyme D641N
0.00042
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.00082
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant mutant C255T
0.0009
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.00111
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant mutant C255T
0.00033
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.00047
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant mutant C255T
0.00084
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Ile-Gly-GLu-Ile-Lys-Glu-Glu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.00154
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Ile-Gly-GLu-Ile-Lys-Glu-Glu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant mutant C255T
0.00024
2-aminobenzoyl-Gly-Pro-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.00036
2-aminobenzoyl-Gly-Pro-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant mutant C255T
0.00219
2-aminobenzoyl-Gly-Pro-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant wild-type enzyme
additional information
additional information
steady-state kinetics and thermodynamics, comparison of human and porcine enzymes, human and porcine PREP have a similar kinetic behavior, overview
-
additional information
additional information
-
steady-state kinetics and thermodynamics, comparison of human and porcine enzymes, human and porcine PREP have a similar kinetic behavior, overview
-
additional information
additional information
-
kinetics and substrate specificity, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1 - 1.1
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
0.6 - 0.9
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
1.4
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant wild-type enzyme
1.4 - 1.5
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
0.6
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Ile-Gly-GLu-Ile-Lys-Glu-Glu-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant wild-type enzyme and mutant C255T
4
2-aminobenzoyl-Gly-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant wild-type enzyme
6
2-aminobenzoyl-Gly-Pro-Phe-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant wild-type enzyme
3.5
2-aminobenzoyl-Gly-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant wild-type enzyme
3.3
2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala-NH2
pH 8.0, wild-type enzyme
5.38
2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala-NH2
pH 8.0, wild-type enzyme
0.0151
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide
pH 7.0, mutant enzyme D641N
0.0657
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide
pH 7.0, mutant enzyme D641A
1
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant mutant C255T
1.1
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant wild-type enzyme
0.6
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant mutant C255T
0.9
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant wild-type enzyme
1.4
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant mutant C255T
1.5
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant wild-type enzyme
1.4
2-aminobenzoyl-Gly-Pro-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant wild-type enzyme
1.8
2-aminobenzoyl-Gly-Pro-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant mutant C255T
7.9
2-aminobenzoyl-Gly-Pro-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37°C, recombinant wild-type enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000036
(2S)-1-[1-(3-[[(2S)-2-(cyclopentylcarbonyl)pyrrolidin-1-yl]carbonyl]benzoyl)-L-prolyl]pyrrolidine-2-carbonitrile
brain
0.000000015
4-phenylbutanoyl-5(R)-tert-butyl-L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine
at 25°C between pH 5.5 and 9.5
0.00000002
4-phenylbutanoyl-L-prolyl-2(S)-cyanopyrrolidine
at 25°C between pH 5.5 and 9.5
0.000000055
benzylcarbamoyl-L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine
at 25°C between pH 5.5 and 9.5
0.00000015
cyclopent-2-ene-1,2-dicarboxylic acid 2-benzylamide 1-[2(S)-(hydroxyacetyl)-H-pyrrolidine]amide
at 25°C between pH 5.5 and 9.5
0.00000015
(2S)-1-[1-[(3-[[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]carbonyl]phenyl)carbonyl]-D-prolyl]pyrrolidine-2-carbaldehyde
-
pH 7.0, 23°C
0.00000039
(2S)-1-[1-[(3-[[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]carbonyl]phenyl)carbonyl]-L-prolyl]pyrrolidine-2-carbonitrile
-
pH 7.0, 23°C
0.0000118
(2S,2'S)-1,1'-(benzene-1,3-diyldicarbonyl)bis[2-(pyrrolidin-1-ylcarbonyl)pyrrolidine]
-
pH 7.0, 23°C
0.000000079
2-hydroxy-1-[(2S)-1-[1-[(3-[[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]carbonyl]phenyl)carbonyl]-D-prolyl]pyrrolidin-2-yl]ethanone
-
pH 7.0, 23°C
0.000000026
4-phenylbutanoyl-5(R)-methyl-L-Pro-2(S)-(hydroxyacetyl)pyrrolidine
-
pH 7.0, 30°C
0.000000022
4-phenylbutanoyl-5(R)-t-butyl-L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine
-
pH 7.0, 23°C
0.000000015
4-phenylbutanoyl-5(R)-tert-butyl-L-Pro-2(S)-(hydroxyacetyl)-pyrrolidine
-
pH 7.0, 30°C
0.000000018
4-phenylbutanoyl-L-Pro-2(S)-(hydroxyacetyl)-pyrrolidine
-
pH 7.0, 30°C
0.000000048
isophthalic acid 2(S)-(cyclopentanecarbonyl)pyrrolidine-L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine amide
-
pH 7.0, 23°C
0.00000036
isophthalic acid 2(S)-(cyclopentanecarbonyl)pyrrolidine-L-prolyl-2(S)-cyanopyrrolidine amide
-
pH 7.0, 23°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000087
(2S)-1-[1-(4-phenylbutanoyl)-L-prolyl]pyrrolidine-2-carbaldehyde
Sus scrofa
kidney
0.000000023
(2S)-1-[1-(4-phenylbutanoyl)-L-prolyl]pyrrolidine-2-carbonitrile
Sus scrofa
-
0.00000088
1-(3-oxo-3-[(2S)-2-(pyrrolidinocarbonyl)pyrrolidin-1-yl]propyl)-3-phenylquinoxalin-2(1H)-one
Sus scrofa
-
0.000059
1-(4-oxo-4-[(2S)-2-(pyrrolidinocarbonyl)pyrrolidin-1-yl]butyl)-3-phenylquinoxalin-2(1H)-one
Sus scrofa
-
0.00011
1-(cyclopent-1-en-1-ylcarbonyl)-N-(2-phenylethyl)-L-prolinamide
Sus scrofa
brain
0.0000021
1-[(2R,5S)-2-(propan-2-yl)-5-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]-4-(pyridin-3-yl)butan-1-one
Sus scrofa
brain
0.0000012
1-[(2R,5S)-2-tert-butyl-5-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]-4-phenylbutan-1-one
Sus scrofa
brain
0.00000081
2-(3-[(2S)-4,4-difluoro-2-(pyrrolidinocarbonyl)pyrrolidin-1-yl]-3-oxopropyl) isoindole-1,3(2H)-dione
Sus scrofa
-
0.00004
2-(4-oxo-4-[(2S)-2-(pyrrolidinocarbonyl)pyrrolidin-1-yl]butyl)-1H-isoindole-1,3(2H)-dione
Sus scrofa
-
0.000003
2-[3-oxo-3-[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]propyl]-1H-isoindole-1,3(2H)-dione
Sus scrofa
-
0.000041
3-(4-oxo-4-[(2S)-2-(pyrrolidinocarbonyl)pyrrolidin-1-yl]butyl)-5,5-diphenylimidazolidine-2,4-dione
Sus scrofa
-
0.00000107
3-cyclohexyl-N-[(2S)-1-oxo-3-phenyl-1-[(2S)-2-(piperidin-1-ylcarbonyl)pyrrolidin-1-yl]propan-2-yl]propanamide
Sus scrofa
kidney
0.000005
4-phenyl-1-[(2S)-2-[[(2S)-2-(1,3-thiazol-2-ylcarbonyl)pyrrolidin-1-yl]carbonyl]pyrrolidin-1-yl]butan-1-one
Sus scrofa
kidney
0.00023
4-phenyl-1-[2-(pyrrolidin-1-ylcarbonyl)cyclopent-1-en-1-yl]butan-1-one
Sus scrofa
brain
0.0000013
4-phenyl-1-[5-(pyrrolidin-1-ylcarbonyl)cyclopent-1-en-1-yl]butan-1-one
Sus scrofa
brain
0.00000026
4-phenylbutanoyl-5(R)-tert-butyl-L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine
Sus scrofa
at 25°C between pH 5.5 and 9.5
0.0000002
4-phenylbutanoyl-L-prolyl-2(S)-cyanopyrrolidine
Sus scrofa
at 25°C between pH 5.5 and 9.5
0.00000083
benzylcarbamoyl-L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine
Sus scrofa
at 25°C between pH 5.5 and 9.5
0.0000003
cyclopent-2-ene-1,2-dicarboxylic acid 2-benzylamide 1-[2(S)-(hydroxyacetyl)-H-pyrrolidine]amide
Sus scrofa
at 25°C between pH 5.5 and 9.5
0.00000105
N-[(2S)-3-methyl-1-oxo-1-[(2S)-2-(piperidin-1-ylcarbonyl)pyrrolidin-1-yl]butan-2-yl]-3-phenoxybenzamide
Sus scrofa
kidney
0.000029
tert-butyl (2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidine-1-carboxylate
Sus scrofa
brain
0.000003
1-(4-phenylbutanoyl)-2(S)-(thiophene-2-carbonyl)pyrrolidin
Sus scrofa
-
pH 7.0, 30°C
0.000059
2(S)-(cyclohex-1-enecarbonyl)-1-(4-phenylbutanoyl)pyrrolidine
Sus scrofa
-
pH 7.0, 30°C
0.000003
2(S)-(cyclopent-1-enecarbonyl)-1-(4-phenylbutanoyl)pyrrolidine
Sus scrofa
-
pH 7.0, 30°C
0.00046
3-(2(S)-benzoyl-pyrrolidine-1-carbonyl)-benzoyl-5(R)-tert-butyl-L-Pro-pyrrolidine
Sus scrofa
-
IC50: 460 nM
0.000018
3-(2(S)-benzoyl-pyrrolidine-1-carbonyl)-benzoyl-L-Pro-pyrrolidine
Sus scrofa
-
IC50: 18 nM
0.00026
4-phenylbutanoyl-2(S)-(2-oxocyclopentanecarbonyl)-pyrrolidine
Sus scrofa
-
IC50: 260 nM
0.00000015
4-phenylbutanoyl-5(R)-methyl-L-Pro-2(S)-(hydroxyacetyl)pyrrolidine
Sus scrofa
-
IC50: 0.15 nM
0.00000026
4-phenylbutanoyl-5(R)-tert-butyl-L-Pro-2(S)-(hydroxyacetyl)-pyrrolidine
Sus scrofa
-
IC50: 0.26 nM
0.00000024
4-phenylbutanoyl-L-Pro-2(S)-(hydroxyacetyl)-pyrrolidine
Sus scrofa
-
IC50: 0.24 nM
0.0000002
4-phenylbutanoyl-L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine
Sus scrofa
-
IC50: 0.2 nM
0.000054
isophthalic acid (L-proline methyl ester) L-prolyl-pyrrolidine amide
Sus scrofa
-
IC50: 54 nM
0.00064
isophthalic acid 2(S)-(cyclopentanecarbonyl)pyrrolidine (L-proline methyl ester) amide
Sus scrofa
-
IC50: 640 nM
0.00000061
isophthalic acid 2(S)-(cyclopentanecarbonyl)pyrrolidine L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine amide
Sus scrofa
-
IC50: 0.61 nM, log P: 0.2, the log P value is a first prediction of the blood-brain barrier penetrability
0.000014
isophthalic acid 2(S)-(cyclopentylcarbonyl)pyrrolidine L-prolyl-pyrrolidine amide
Sus scrofa
-
IC50: 14 nM, log P: 1.1, the log P value is a first prediction of the blood-brain barrier penetrability
0.00000072
isophthalic acid 2(S)-(cylcohexanecarbonyl)pyrrolidine L-prolyl-2(S)-cynaopyrrolidine amide
Sus scrofa
-
IC50: 0.72 nM
0.0000011
isophthalic acid 2(S)-(cylcopentanecarbonyl)pyrrolidine L-prolyl-2(S)-cynaopyrrolidine amide
Sus scrofa
-
IC50: 1.1 nM, log P: 0.8, the log P value is a first prediction of the blood-brain barrier penetrability
0.0000012
isophthalic acid 2(S)-acetylpyrrolidine L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine amide
Sus scrofa
-
IC50: 1.2 nM
0.0000042
isophthalic acid 2(S)-acetylpyrrolidine L-prolyl-2(S)-cynaopyrrolidine amide
Sus scrofa
-
IC50: 4.2 nM, log P: -0.6, the log P value is a first prediction of the blood-brain barrier penetrability
0.000065
isophthalic acid 2(S)-acetylpyrrolidine L-prolyl-pyrrolidine amide
Sus scrofa
-
IC50: 65 nM
0.0000013
isophthalic acid 2(S)-benzoylpyrrolidine L-prolyl-2(S)-cynaopyrrolidine amide
Sus scrofa
-
IC50: 1.3 nM, log P: 1.1, the log P value is a first prediction of the blood-brain barrier penetrability
0.000018
isophthalic acid 2(S)-benzoylpyrrolidine L-prolyl-pyrrolidine amide
Sus scrofa
-
IC50: 18 nM
0.0000016
isophthalic acid 2(S)-isobutanoylpyrrolidine L-prolyl-2(S)-cynaopyrrolidine amide
Sus scrofa
-
IC50: 1.6 nM, log P: 0.3, the log P value is a first prediction of the blood-brain barrier penetrability
0.000078
isophthalic acid bis-2(S)-(cyclopentanecarbonyl)pyrrolidine amide
Sus scrofa
-
IC50: 78 nM, log P: 2.7, the log P value is a first prediction of the blood-brain barrier penetrability
0.00000039
isophthalic acid L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine L-prolyl-pyrrolidine amide
Sus scrofa
-
IC50: 0.39 nM
0.0000015
isophthalic acid L-prolyl-2(S)-cyanopyrrolidine L-prolyl-pyrrolidine amide
Sus scrofa
-
IC50: 1.5 nM
0.0000013
isophthalic acid L-prolyl-pyrrolidine L-prolyl-L-prolinal amide
Sus scrofa
-
IC50: 1.3 nM
0.000031
isophthalic acid L-prolylbenzylamine L-prolyl-pyrrolidine amide
Sus scrofa
-
IC50: 31 nM
0.000026
isophthalic acid bis(L-prolyl-pyrrolidine) amide
Sus scrofa
-
IC50: 26 nM, log O = -0.2, the log P value is a first prediction of the blood-brain barrier penetrability
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00017
-
high-density membranes, membrane-bound POP activity of different-density membrane fractions obtained by sucrose gradient centrifugation
0.0002
-
washed membranes, POP activity partitioning during membrane preparation crude extract and membrane wash effects on recovered activity
0.00045
-
medium-density membranes, membrane-bound POP activity of different-density membrane fractions obtained by sucrose gradient centrifugation
0.0005
0.00061
-
low-density membranes, membrane-bound POP activity of different-density membrane fractions obtained by sucrose gradient centrifugation
0.001
-
crude extract, POP activity partitioning during membrane preparation crude extract and membrane wash effects on recovered activity
0.0014
-
unwashed membranes, POP activity partitioning during membrane preparation crude extract and membrane wash effects on recovered activity
0.0033
-
Triton X-100 extraction, purification of mPOP from a total membrane preparation
0.0048
-
4 M NaCl wash, POP activity partitioning during membrane preparation crude extract and membrane wash effects on recovered activity
0.009
-
0.5 M NaCl wash, POP activity partitioning during membrane preparation crude extract and membrane wash effects on recovered activity
0.0138
-
water wash, POP activity partitioning during membrane preparation crude extract and membrane wash effects on recovered activity
additional information
0.0005
-
washed membranes, membrane-bound POP activity of different-density membrane fractions obtained by sucrose gradient centrifugation
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.9
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
participates in several aspects and functions of the central nervous system, including learning, memory, mood, hypertension and eating, and in some neurodegenerative diseases such as Alzheimer`s and Parkinson`s diseases
malfunction
-
enzyme associated with schizophrenia, bipolar affective disorder and related neuropsychiatric disorders
additional information
additional information
human PREP behaves identically to the porcine homologue, displaying a double bell-shaped pH profile and a pH-dependent solvent kinetic isotope effect of the kcat/Km, features that set it apart from the related exopeptidase dipeptidyl peptidase IV (DPP IV)
additional information
-
human PREP behaves identically to the porcine homologue, displaying a double bell-shaped pH profile and a pH-dependent solvent kinetic isotope effect of the kcat/Km, features that set it apart from the related exopeptidase dipeptidyl peptidase IV (DPP IV)
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PPCE_PIG
710
0
80770
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65000
-
higher salt concentrations used, membrane PE activity elutes with a molecular mass of 65 kDa
80000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme consists of two domains, a peptidase and a seven-bladed beta-propeller, the peptidase domain exhibits an alpha/beta-hydrolase fold contains a central eight-stranded beta-sheet, the beta-propeller of POP is held to the catalytic domain via the two connecting polypeptide main chains, with hydrogen bonds and salt bridges, but mainly with hydrophobic forces
additional information
the enzyme structure contains two domains, the peptidase domain consitst of N- and C-terminal residues 1-72 and 428-710 containing the catalytic triad Ser554, Asp641, and His680 and is arranged in a classical alpha/beta hydrolase fold, the seven-bladed beta-propeller domain, residues 73-427, is radially arranged around the central tunnel embedded within the cylinder, where the narrow active site is located
additional information
-
the enzyme has a two-domain structure whose unique seven-blade beta-propeller domain works with the catalytic domain, mechanism for peptide entry between the two domains, the flexible loop region of the propeller domain, residues 192-205, that interacts with the catalytic domain, has the highest flexibility within the enzyme, molecular dynamics analysis, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
limited proteolysis of the porcine enzyme with trypsin reveals a cleavage site at the Lys196-Ser197 bond in the flexible loop region of the propeller domain that interacts with the catalytic domain
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
D641A and D641N mutants are cocrystallized in presence of substrate benzyloxycarbonyl-Gly-Pro-4-nitroanilide
enzyme in complex with inhibitor benzyloxycarbonyl-Pro-Prolinal, X-ray diffraction structure determination at high resolution
peptides 2-aminobenzoyl-Gly-Phe-Arg-Pro-Phe(NO2)-Arg-Ala, 2-aminobenzoyl-Gly-Phe-Glu-Pro-Phe(NO2)-Arg-Ala or 2-aminobenzoyl-Glu-Phe-Ser-Pro-Phe(NO2)-Arg-Ala with prolyl oligopeptidase
S554A mutant enzyme cocrystallized with 2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala-NH2 or benzyloxycarbonyl-Gly-Pro-beta-naphthylamide
wild-type enzyme, mutant enzyme Y473F, mutant enzyme Y473F + benzyloxcarbonyl-Pro-prolinal and mutant enzyme S554A + succinyl-Gly-Pro-OH
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D641A
the ratio of turnover number to Km-value for the substrate benzyloxycarbonyl-Gly-Pro-beta-naphthylamide is 0.2% of the wild-type ratio. The ratio of turnover number to Km-value for the substrate 2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala-NH2 is 1.8fold higher than the wild-type ratio. The ratio of turnover number to Km-value for the substrate benzyloxycarbonyl-Gly-Pro-p-nitrophenol is 66% of the wild-type ratio. The ratio of turnover number to Km-value for the substrate benzyloxycarbonyl-Gly-Pro-SBzl is 0.92% of the wild-type ratio
D641N
the ratio of turnover number to Km-value for the substrate benzyloxycarbonyl-Gly-Pro-beta-naphthylamide is 0.02% of the wild-type ratio. The ratio of turnover number to Km-value for the substrate 2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala-NH2 is 1.4fold higher than the wild-type ratio. The ratio of turnover number to Km-value for the substrate benzyloxycarbonyl-Gly-Pro-p-nitrophenol is 40% of the wild-type ratio. The ratio of turnover number to Km-value for the substrate benzyloxycarbonyl-Gly-Pro-SBzl is 0.27% of the wild-type ratio
R252S
specificity rate constant for 2-aminobenzoyl-Gly-Glu-Ser-Pro-Phe(NO2)-Arg-Ala is 39% of the wild-type value, for 2-aminobenzoyl-Glu-Phe-Ser-Pro-Phe(NO2)-Arg-Ala nearly identical to wild-type value, for 2-aminobenzoyl-Glu-Gly-Phe-Ser-Pro-Phe(NO2)-Arg-Ala 52% of wild-type value, for benzyloxycarbonyl-Gly-Pro-beta-naphthylamide 78% of the wild-type value
Y473F
catalysis by the wild-type enzyme exhibits positive activation entropy. In contrast the activation entropy for the mutant enzyme is negative
C255T
-
site-directed mutagenesis, mutant substrate specificity and kinetics in comparison to the wild-type enzyme
additional information
expression of beta-propeller domain of enzyme as a stable, soluble protein with seven blades. Propeller domain is more stable than parent prolyl oligopeptidase. Deletion of the seventh blade of the propeller leads to a stable six-bladed propeller that dimerizes in contrast to the monomeric seven-bladed propeller
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged full-length and truncated brain enzymes in Escherichia coli strain JM105
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
positive effect of prolyl oligopeptidase inhibitors on learning and memory in animal models for amnesia, enzyme activity measurements in patient samples and (neuro)peptide degradation studies link the enzyme with neurodegenerative disorders
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hauzer, K.; Servitova, L.; Barth, T.; Jost, K.
Post-proline endopeptidase. Partial purification and characterization of the enzyme from pig kidneys
Collect. Czech. Chem. Commun.
47
1139-1148
1982
Sus scrofa
-
Hauzer, K.; Barth, T.; Servitova, L.; Jost, K.
Post-proline endopeptidase. Further characterization of the enzyme from pig kidneys
Collect. Czech. Chem. Commun.
49
1846-1853
1984
Sus scrofa
-
Bocskei, Z.; Fuxreiter, M.; Naray-Szabo, G.; Szabo, E.; Polar, L.
Crystallization and preliminary X-ray analysis of porcine muscle prolyl oligopeptidase
Acta Crystallogr. Sect. D
54
1414-1415
1998
Sus scrofa
Hauzer, K.; Barth, T.; Jost, K.; Barthova, J.; Hauzerova, L.
Endoprolylpeptidase (EC 3.4.21.26), improvement of the isolation method
Collect. Czech. Chem. Commun.
52
522-524
1987
Sus scrofa
-
Moriyama, A.; Nakanishi, M.; Takenaka, O.; Sasaki, M.
Porcine muscle prolyl endopeptidase: limited proteolysis of tryptic peptides from hemoglobin beta-chains at prolyl and alanyl bonds
Biochim. Biophys. Acta
956
151-155
1988
Sus scrofa
Schoenlein, C.; Heins, J.; Barth, A.
Purification and characterization of prolyl endopeptidase from pig brain
Biol. Chem.
371
1159-1164
1990
Sus scrofa
Wallen, E.A.; Christiaans, J.A.; Saario, S.M.; Forsberg, M.M.; Venalainen, J.I.; Paso, H.M.; Mannisto, P.T.; Gynther, J.
4-Phenylbutanoyl-2(S)-acylpyrrolidines and 4-phenylbutanoyl-L-prolyl-2(S)-acylpyrrolidines as prolyl oligopeptidase inhibitors
Bioorg. Med. Chem.
10
2199-2206
2002
Sus scrofa
Wallen, E.A.; Christiaans, J.A.; Saarinen, T.J.; Jarho, E.M.; Forsberg, M.M.; Venalainen, J.I.; Mannisto, P.T.; Gynther, J.
Conformationally rigid N-acyl-5-alkyl-L-prolyl-pyrrolidines as prolyl oligopeptidase inhibitors
Bioorg. Med. Chem.
11
3611-3619
2003
Sus scrofa
Flp, V.; Szeltner, Z.; Renner, V.; Polgar, L.
Structures of prolyl oligopeptidase substrate/inhibitor complexes. Use of inhibitor binding for titration of the catalytic histidine residue
J. Biol. Chem.
276
1262-1266
2001
Sus scrofa (P23687)
Szeltner, Z.; Rea, D.; Renner, V.; Fulop, V.; Polgar, L.
Electrostatic effects and binding determinants in the catalysis of prolyl oligopeptidase. Site specific mutagenesis at the oxyanion binding site
J. Biol. Chem.
277
42613-42622
2002
Sus scrofa (P23687)
Szeltner, Z.; Rea, D.; Juhasz, T.; Renner, V.; Mucsi, Z.; Orosz, G.; Fulop, V.; Polgar, L.
Substrate-dependent competency of the catalytic triad of prolyl oligopeptidase
J. Biol. Chem.
277
44597-44605
2002
Sus scrofa (P23687)
Szeltner, Z.; Rea, D.; Renner, V.; Juliano, L.; Fulop, V.; Polgar, L.
Electrostatic environment at the active site of prolyl oligopeptidase is highly influential during substrate binding
J. Biol. Chem.
278
48786-48793
2003
Sus scrofa (P23687)
Wallen, E.A.; Christiaans, J.A.; Forsberg, M.M.; Venalainen, J.I.; Mannisto, P.T.; Gynther, J.
Dicarboxylic acid bis(L-prolyl-pyrrolidine) amides as prolyl oligopeptidase inhibitors
J. Med. Chem.
45
4581-4584
2002
Sus scrofa
Wallen, E.A.; Christiaans, J.A.; Jarho, E.M.; Forsberg, M.M.; Venalainen, J.I.; Mannisto, P.T.; Gynther, J.
New prolyl oligopeptidase inhibitors developed from dicarboxylic acid bis(l-prolyl-pyrrolidine) amides
J. Med. Chem.
46
4543-4551
2003
Pyrococcus furiosus, Sus scrofa
Besedin, D.V.; Rudenskaya, G.N.
Proline-specific endopeptidases
Russ. J. Bioorg. Chem.
29
1-17
2003
Agaricus bisporus, Bos taurus, Cavia porcellus, Gallus gallus, Elizabethkingia meningoseptica, Oryctolagus cuniculus, Novosphingobium capsulatum, Ovis aries, Homo sapiens, Lyophyllum cinerascens, Mus musculus, Rattus norvegicus, Sus scrofa, Xanthomonas sp., Ascidia sp., Clupea pallasii, Lactifluus hygrophoroides, Russula lepida
-
Venaelaeinen, J.I.; Juvonen, R.O.; Garcia-Horsman, J.A.; Wallen, E.A.; Christiaans, J.A.; Jarho, E.M.; Gynther, J.; Maennistoe, P.T.
Slow-binding inhibitors of prolyl oligopeptidase with different functional groups at the P1 site
Biochem. J.
382
1003-1008
2004
Sus scrofa
Venaelaeinen, J.I.; Garcia-Horsman, J.A.; Forsberg, M.M.; Jalkanen, A.; Wallen, E.A.; Jarho, E.M.; Christiaans, J.A.; Gynther, J.; Maennistoe, P.T.
Binding kinetics and duration of in vivo action of novel prolyl oligopeptidase inhibitors
Biochem. Pharmacol.
71
683-692
2006
Sus scrofa
Jarho, E.M.; Wallen, E.A.; Christiaans, J.A.; Forsberg, M.M.; Venaelaeinen, J.I.; Maennistoe, P.T.; Gynther, J.; Poso, A.
Dicarboxylic acid azacycle l-prolyl-pyrrolidine amides as prolyl oligopeptidase inhibitors and three-dimensional quantitative structure-activity relationship of the enzyme-inhibitor interactions
J. Med. Chem.
48
4772-4782
2005
Sus scrofa (P23687), Sus scrofa
Juhasz, T.; Szeltner, Z.; Fueloep, V.; Polgar, L.
Unclosed beta-propellers display stable structures: implications for substrate access to the active site of prolyl oligopeptidase
J. Mol. Biol.
346
907-917
2005
Sus scrofa (P23687)
Jarho, E.M.; Venaelaeinen, J.I.; Poutiainen, S.; Leskinen, H.; Vepsaelaeinen, J.; Christiaans, J.A.; Forsberg, M.M.; Maennistoe, P.T.; Wallen, E.A.
2(S)-(Cycloalk-1-enecarbonyl)-1-(4-phenyl-butanoyl)pyrrolidines and 2(S)-(aroyl)-1-(4-phenylbutanoyl)pyrrolidines as prolyl oligopeptidase inhibitors
Bioorg. Med. Chem.
15
2024-2031
2007
Sus scrofa
Gass, J.; Khosla, C.
Prolyl endopeptidases
Cell. Mol. Life Sci.
64
345-355
2007
Elizabethkingia meningoseptica, Dictyostelium discoideum, Novosphingobium capsulatum, Homo sapiens, Mus musculus, Myxococcus xanthus, Pyrococcus furiosus, Rattus norvegicus, Sus scrofa
Szeltner, Z.; Polgar, L.
Structure, function and biological relevance of prolyl oligopeptidase
Curr. Protein Pept. Sci.
9
96-107
2008
Elizabethkingia meningoseptica, Dictyostelium discoideum, Novosphingobium capsulatum, Homo sapiens, Platyrrhini, Mus musculus, Myxococcus xanthus, Pyrococcus furiosus, Rattus norvegicus, Sus scrofa
Garcia-Horsman, J.A.; Maennistoe, P.T.; Venaelaeinen, J.I.
On the role of prolyl oligopeptidase in health and disease
Neuropeptides
41
1-24
2007
Dictyostelium discoideum, Novosphingobium capsulatum, Flavobacterium sp., Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa (P23687)
Gorrao, S.S.; Hemerly, J.P.; Lima, A.R.; Melo, R.L.; Szeltner, Z.; Polgar, L.; Juliano, M.A.; Juliano, L.
Fluorescence resonance energy transfer (FRET) peptides and cycloretro-inverso peptides derived from bradykinin as substrates and inhibitors of prolyl oligopeptidase
Peptides
28
2146-2154
2007
Sus scrofa
Juhasz, T.; Szeltner, Z.; Polgar, L.
Truncated prolyl oligopeptidase from Pyrococcus furiosus
Proteins
69
633-643
2007
Pyrococcus furiosus, Sus scrofa (P23687)
Tenorio-Laranga, J.; Venaelaeinen, J.I.; Maennistoe, P.T.; Garcia-Horsman, J.A.
Characterization of membrane-bound prolyl endopeptidase from brain
FEBS J.
275
4415-4427
2008
Sus scrofa
Kanai, K.; Aranyi, P.; Boecskei, Z.; Ferenczy, G.; Harmat, V.; Simon, K.; Batori, S.; Naray-Szabo, G.; Hermecz, I.
Prolyl oligopeptidase inhibition by N-acyl-pro-pyrrolidine-type molecules
J. Med. Chem.
51
7514-7522
2008
Sus scrofa (P23687)
Brandt, I.; Gerard, M.; Sergeant, K.; Devreese, B.; Baekelandt, V.; Augustyns, K.; Scharpe, S.; Engelborghs, Y.; Lambeir, A.M.
Prolyl oligopeptidase stimulates the aggregation of alpha-synuclein
Peptides
29
1472-1478
2008
Sus scrofa
Tarrag, T.; Claasen, B.; Kichik, N.; Rodriguez-Mias, R.; Gair, M.; Giralt, E.
A cost-effective labeling strategy for the NMR study of large proteins: Selective 15N-labeling of the tryptophan side chains of prolyl oligopeptidase
ChemBioChem
10
2736-2739
2009
Sus scrofa
Lawandi, J.; Gerber-Lemaire, S.; Juillerat-Jeanneret, L.; Moitessier, N.
Inhibitors of prolyl oligopeptidases for the therapy of human diseases: Defining diseases and inhibitors
J. Med. Chem.
53
3423-3438
2010
Bos taurus, Canis lupus familiaris, Elizabethkingia meningoseptica, Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa (P23687)
Tenorio-Laranga, J.; Coret-Ferrer, F.; Casanova-Estruch, B.; Burgal, M.; Garcia-Horsman, J.A.
Prolyl oligopeptidase is inhibited in relapsing-remitting multiple sclerosis
J. Neuroinflammation
7
23
2010
Homo sapiens, Sus scrofa
Comellas, G.; Kaczmarska, Z.; Tarrag, T.; Teixid, M.; Giralt, E.
Exploration of the one-bead one-compound methodology for the design of prolyl oligopeptidase substrates
PLoS ONE
4
e6222
2009
Sus scrofa
Kaszuba, K.; Rog, T.; Danne, R.; Canning, P.; Fueloep, V.; Juhasz, T.; Szeltner, Z.; St Pierre, J.F.; Garcia-Horsman, A.; Maennistoe, P.T.; Karttunen, M.; Hokkanen, J.; Bunker, A.
Molecular dynamics, crystallography and mutagenesis studies on the substrate gating mechanism of prolyl oligopeptidase
Biochimie
94
1398-1411
2012
Sus scrofa (P23687)
Savolainen, M.H.; Yan, X.; Myoehaenen, T.T.; Huttunen, H.J.
Prolyl oligopeptidase enhances alpha-synuclein dimerization via direct protein-protein interaction
J. Biol. Chem.
290
5117-5126
2015
Sus scrofa
Kaushik, S.; Etchebest, C.; Sowdhamini, R.
Decoding the structural events in substrate-gating mechanism of eukaryotic prolyl oligopeptidase using normal mode analysis and molecular dynamics simulations
Proteins
82
1428-1443
2014
Aeromonas caviae, Myxococcus xanthus, Sus scrofa (P23687), Sus scrofa, Novosphingobium capsulatum (Q9ZNM8)
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