Any feedback?
Information on EC 3.4.21.26 - prolyl oligopeptidase and Organism(s) Homo sapiens and UniProt Accession P48147
for references in articles please use BRENDA:EC3.4.21.26Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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: Homo sapiens
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-
-
-
-
-
POP
-
-
post-proline cleaving enzyme
post-proline endopeptidase
postproline endopeptidase
-
-
-
-
postproline-cleaving enzyme
-
-
-
-
proline endopeptidase
-
-
-
-
proline-specific endopeptidase
-
-
-
-
prolyl endopeptidase
prolyl oligopeptidase
-
-
additional information
post-proline cleaving enzyme
-
-
-
-
post-proline endopeptidase
-
-
-
-
prolyl endopeptidase
-
-
-
-
prolyl endopeptidase
-
-
additional information
-
the enzyme belongs to the POP family of serine proteases, family S9 of clan SC
additional information
-
the enzyme is a member of the prolyl oligopeptidase family, subfamily S9a
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
catalytic mechanism, structure-function relationship, the enzyme contains a Ser-Asp-His catalytic triad, substrate specificity and binding structure,overview
-
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
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
-
-
-
?
(S)-benzyl 2-(2-(4-hydroxynaphthalen-1-ylcarbamoyl)pyrrolidin-1-yl)-2-oxoethylcarbamate + H2O
?
-
specific substrate, UAMC-00682
-
-
?
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-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-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-Ala-Ala-Pro-4-nitrophenylalanine + H2O
Abz-Ala-Ala-Pro + 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 10% 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-Gly-Gly-Pro-4-nitrophenylalanine + H2O
Abz-Gly-Gly-Pro + 4-nitrophenylalanine
-
about 2% activity compared to Abz-Lys-Pro-4-nitrophenylalanine
-
-
?
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
-
-
-
-
?
Abz-Gly-Pro-4-nitrophenylalanine + H2O
Abz-Gly-Pro + 4-nitrophenylalanine
-
about 7% activity compared to Abz-Lys-Pro-4-nitrophenylalanine
-
-
?
Abz-Lys-Pro-4-nitrophenylalanine + H2O
Abz-Lys-Pro + 4-nitrophenylalanine
-
100% activity
-
-
?
alpa2-antiplasmin + H2O
?
-
not a robust substrate in vitro, the enzyme cleaves after Pro12 in the T9S10G11P12-N13 Q14E15Q16E17 sequence
-
-
?
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
-
-
-
-
?
collagen + H2O
N-acetyl-Pro-Gly-Pro + ?
-
after enzyme activation with LPS
-
-
?
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
-
-
?
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
-
?
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-carbobenzoxy-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
N-carbobenzoxy-Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
N-carbobenzyloxy-Ala-Pro-2-naphthylamide + H2O
N-carbobenzyloxy-Ala-Pro + 2-naphthylamine
-
-
-
-
?
N-succinyl-Ala-Ala-Ala-4-nitroanilide
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
-
-
-
-
?
N-succinyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
N-succinyl-Gly-L-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-prolyl-7-amido-4-methylcoumarin + H2O
N-succinyl-glycyl-prolyl + 7-amino-4-methylcoumarin
-
-
-
-
?
Peptides + H2O
?
-
metabolism of peptides containing altered aspartyl residues
-
-
?
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-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
-
about 58% activity compared to Z-Gly-L-Pro-7-amido-4-methylcoumarin
-
-
?
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-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-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-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-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-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
Z-Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
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-methylcoumarin
Z-Gly-Pro + 7-amino-4-methylcoumarin
-
assay at pH 8.0, 37°C, reaction stopped with sodium acetate
-
-
?
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-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-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-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-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-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-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-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-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-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-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
-
-
?
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
-
-
?
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
alpa2-antiplasmin + H2O
?
-
not a robust substrate in vitro, the enzyme cleaves after Pro12 in the T9S10G11P12-N13 Q14E15Q16E17 sequence
-
-
?
membrane-associated glycoprotein neural cell adhesion molecule + H2O
?
-
-
-
-
?
Peptides + H2O
?
-
metabolism of peptides containing altered aspartyl residues
-
-
?
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
?
-
-
cleaves short proline-containing neuropeptides, and is involved in memory and learning
-
-
?
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S)-1-[[(2S)-1-(1-oxo-4-phenylbutyl)-2-pyrrolidinyl]carbonyl]-2-pyrrolidinecarbonitrile
i.e. KYP-2047, hyperbolic kinetics of KYP-2047 binding to human PREP with pseudo-firstorder rate constant, Van't Hoff plot for binding of KYP-2047 to human PREP, a covalent bond is formed between the nitrile group of KYP-2047 and the active site serine
((8'Z)-pentadecenyl)-salicylic acid
-
a noncompetitive inhibitor isolated from Gingko biloba leaves
(1R,3S,4S,5S)-1,3,4-tris(acetyloxy)-5-([(2E)-3-[3,4-bis(acetyloxy)phenyl]prop-2-enoyl]oxy)cyclohexanecarboxylic acid
-
81.9% inhibition at 0.5 mM
(1R,3S,4S,5S)-3-[[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy]-1,4,5-trihydroxycyclohexanecarboxylic acid
-
88% inhibition at 0.5 mM
(2S)-1-({(2S,4S)-4-[2-(1,3-Dihydro-2H-isoindol-2-yl)-2-oxo- ethyl]-5-oxopyrrolidin-2-yl}carbonyl)-4,4-difluoropyrrolidine-2- carbonitrile
-
potent and selective inhibitor of FAP, 0.01 mM used in assay conditions
(2S,3aS,7aS)-1-[[(1R,2R)-2-phenylcyclopropyl]carbonyl]-2-(1,3-thiazolidin-3-ylcarbonyl)octahydro-1H-indole
-
S-17092
(3S)-3-(pyrrolidin-1-ylcarbonyl)-6-[[4-(trifluoromethyl)benzyl]oxy]-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-6-[(2,4-difluorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-6-[(2,5-difluorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-6-[(3,4-difluorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-6-[(3,5-difluorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-6-[(3,5-difluorobenzyl)oxy]-8-(phenylsulfonyl)-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-6-[(4-fluorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-6-[(4-tert-butylbenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-6-[(4-tert-butylbenzyl)oxy]-8-(phenylsulfonyl)-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-8-(phenylsulfonyl)-3-(pyrrolidin-1-ylcarbonyl)-6-[[4-(trifluoromethyl)benzyl]oxy]-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-8-acetyl-3-(pyrrolidin-1-ylcarbonyl)-6-(2,2,2-trifluoroethoxy)-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-8-acetyl-3-(pyrrolidin-1-ylcarbonyl)-6-[[4-(trifluoromethyl)benzyl]oxy]-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-8-acetyl-6-(2-phenylethyl)-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-8-acetyl-6-[(3,4-dichlorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-8-acetyl-6-[(3,4-difluorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-8-acetyl-6-[(3,5-difluorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-8-acetyl-6-[(3-chloro-4-fluorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-8-acetyl-6-[(4-chlorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-8-acetyl-6-[(4-fluorobenzyl)oxy]-3-(1H-pyrazol-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-8-acetyl-6-[(4-fluorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-8-acetyl-6-[(4-methoxybenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
-
-
(3S)-8-acetyl-6-[2-(4-fluorophenyl)ethyl]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
-
-
(5R,7S,8S,9S)-8,9-dihydroxy-2,2-dimethyl-4-oxo-1,3-dioxaspiro[4.5]dec-7-yl (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
-
88.3% inhibition at 0.5 mM
(6S)-1,3-dichloro-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
-
-
(6S)-1-chloro-3-(cyclohexylmethoxy)-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
-
-
(6S)-1-chloro-3-(naphthalen-2-ylmethoxy)-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
-
-
(6S)-1-chloro-3-(pyridin-4-ylmethoxy)-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
-
-
(6S)-1-chloro-3-phenoxy-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
-
-
(6S)-1-chloro-3-[(2-phenylethyl)amino]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
-
-
(6S)-1-chloro-3-[(3,4-dichlorobenzyl)oxy]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
-
-
(6S)-1-chloro-3-[(3,4-difluorobenzyl)amino]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
-
-
(6S)-1-chloro-3-[(3,4-difluorobenzyl)oxy]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
-
-
(6S)-1-chloro-3-[(3-chloro-4-fluorobenzyl)oxy]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
-
-
(6S)-1-chloro-3-[(3-chlorobenzyl)oxy]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
-
-
(6S)-1-chloro-3-[(4-fluorobenzyl)amino]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
-
-
(6S)-1-chloro-3-[(4-fluorobenzyl)oxy]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
(6S)-1-chloro-3-[2-(3,4-dichlorophenyl)ethoxy]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
-
-
(6S)-1-chloro-3-[2-(4-fluorophenyl)ethoxy]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
-
-
(6S)-1-chloro-6-(pyrrolidin-1-ylcarbonyl)-3-[(2,3,5-trifluorobenzyl)oxy]-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
-
-
(6S)-1-chloro-6-(pyrrolidin-1-ylcarbonyl)-3-[[4-(trifluoromethyl)benzyl]oxy]-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
-
-
(6S)-3-(benzylamino)-1-chloro-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
-
-
(E)-1-(3-(4-methoxyphenyl)acryloyl)pyrrolidine-2-carboxylic acid
-
less than 10% inhibition at 0.5 mM
(E)-4-(3-(2-(methoxycarbonyl)pyrrolidin-1-yl)-3-oxoprop-1-enyl)-1,2-phenylene-diacetate
-
98.3% inhibition at 0.5 mM
(E)-methyl 1-(3-(3,4-dihydroxyphenyl)acryloyl)pyrrolidine-2-carboxylate
-
96.3% inhibition at 0.5 mM
(E)-methyl 1-(3-(3-(3,4-dihydroxyphenyl)acryloyloxy)-1,4,5-trihydroxycyclohexanecarbonyl)pyrrolidine-2-carboxylate
-
75.5% inhibition at 0.5 mM
(E)-methyl 1-(3-(4-methoxyphenyl)acryloyl)pyrrolidine-2-carboxylate
-
42.8% inhibition at 0.5 mM
(S)-1-((S)-1-(4-phenylbutanoyl)-pyrrolidine-2-carbonyl)pyrrolidine-2-carbonitrile
-
KYP-2047, most potent inhibitor
1,2,3,4,6-pentagalloyl glucopyranoside
-
specific, noncompetitive, and strong inhibition
1,2,3-trigalloyl glucopyranoside
-
specific, noncompetitive, and strong inhibition
1,2,6-trigalloyl glucopyranoside
-
from Euphorbia helioscopia, specific, noncompetitive, and strong inhibition
1,3-dibenzyl-4-(benzylamino)-5-(methoxycarbonyl)-1H-3,1-benzimidazol-3-ium iodide
-
-
1,3-dicyclohexyl-4-(cyclohexylamino)-5-(methoxycarbonyl)-1H-3,1-benzimidazol-3-ium iodide
-
-
1-benzyl-3-cyclohexyl-4-(cyclohexylamino)-5-(methoxycarbonyl)-1H-3,1-benzimidazol-3-ium iodide
-
-
1-benzyl-3-cyclohexyl-4-(cyclohexylamino)-5-(methoxymethyl)-1H-3,1-benzimidazol-3-ium iodide
-
-
3-({4-[2-(E)-styrylphenoxy]butanoyl}-L-4-hydroxyprolyl)-thiazolidine
-
SUAM-14746, selective prolyl oligopeptidase inhibitor
3-benzyl-4-(benzylamino)-5-(methoxycarbonyl)-1-methyl-1H-3,1-benzimidazol-3-ium iodide
-
-
3-cyclohexyl-4-(cyclohexylamino)-1-ethyl-5-[(prop-2-en-1-yloxy)carbonyl]-1H-3,1-benzimidazol-3-ium iodide
-
-
3-cyclohexyl-4-(cyclohexylamino)-1-methyl-5-[(prop-2-en-1-yloxy)carbonyl]-1H-3,1-benzimidazol-3-ium iodide
-
-
3-cyclohexyl-4-(cyclohexylamino)-5-(methoxycarbonyl)-1-(4-methylphenyl)-1H-3,1-benzimidazol-3-ium iodide
-
-
3-cyclohexyl-4-(cyclohexylamino)-5-(methoxycarbonyl)-1-methyl-1H-3,1-benzimidazol-3-ium iodide
-
-
3-cyclohexyl-4-(cyclohexylamino)-5-(methoxycarbonyl)-1-[(1S)-1-phenylethyl]-1H-3,1-benzimidazol-3-ium iodide
-
-
4-(4-chlorophenyl)-8-(ethoxycarbonyl)-5-methyl-2,3-dihydrofuro[3,2-c]quinolin-5-ium iodide
-
-
4-([[(3S)-8-acetyl-5-oxo-3-(pyrrolidin-1-ylcarbonyl)-1,2,3,5-tetrahydroindolizin-6-yl]oxy]methyl)benzonitrile
-
-
4-phenyl-1-[(3S)-3-(pyrrolidin-1-ylcarbonyl)-3,4-dihydroisoquinolin-2(1H)-yl]butan-1-one
-
-
5-(4-chlorophenyl)-9-(ethoxycarbonyl)-6-methyl-3,4-dihydro-2H-pyrano[3,2-c]quinolin-6-ium iodide
-
-
5-(methoxycarbonyl)-3-(4-methoxyphenyl)-4-[(4-methoxyphenyl)amino]-1-methyl-1H-3,1-benzimidazol-3-ium iodide
-
-
5-cyano-3-cyclohexyl-4-(cyclohexylamino)-1-methyl-1H-3,1-benzimidazol-3-ium iodide
-
-
6-((10'Z)-heptadecenyl)salicylic acid
-
a noncompetitive inhibitor isolated from Gingko biloba leaves
8-(ethoxycarbonyl)-5-methyl-4-naphthalen-1-yl-2,3-dihydrofuro[3,2-c]quinolin-5-ium iodide
-
-
9-(ethoxycarbonyl)-6-methyl-5-phenyl-3,4-dihydro-2H-pyrano[3,2-c]quinolin-6-ium iodide
-
-
benzyl (2S)-2-[(2S)-2-formylpyrrolidine-1-carbonyl]pyrrolidine-1-carboxylate
-
-
benzyl (2S)-2-[[(2S)-2-(hydroxymethyl)pyrrolidin-1-yl]carbonyl]pyrrolidine-1-carboxylate
-
-
benzyl [(2R)-1-[(2S)-2-cyanopyrrolidin-1-yl]-1-oxopropan-2-yl]carbamate
-
0.02 mM, more than 90% inhibition in extracts from brain-derived endothelial cells, extracts from astrocyte-derived cells and extracts from fibroblasts
benzyl [(2R,3R,7aS)-3-cyano-2-methyl-5-oxohexahydropyrrolo[2,1-b][1,3]oxazol-6-yl]carbamate
-
0.1 mM, 10-50% inhibition in extracts from astrocyte-derived cells and extracts from brain-derived endothelial cells, more than 50% inhibition in extracts from brain-derived endothelial cells
benzyl [(2S)-1-[(2S)-2-cyanopyrrolidin-1-yl]-1-oxopropan-2-yl]carbamate
-
0.02 mM, more than 90% inhibition in extracts from brain-derived endothelial cells, extracts from astrocyte-derived cells and extracts from fibroblasts
benzyl [(3R,6R,8aS)-3-cyano-5-oxohexahydro-5H-[1,3]thiazolo[3,2-a]pyridin-6-yl]carbamate
-
0.1 mM, more than 50% inhibition in extracts from astrocyte-derived cells, extracts from brain-derived endothelial cells and extracts from fibroblasts
benzyl [(3R,6S,7aS)-3-cyano-5-oxohexahydropyrrolo[2,1-b][1,3]thiazol-6-yl]carbamate
-
0.1 mM, 10-50% inhibition in extracts from astrocyte-derived cells and extracts from brain-derived endothelial cells, more than 50% inhibition in extracts from brain-derived endothelial cells
benzyl [(3R,6S,8aS)-3-cyano-5-oxohexahydro-5H-[1,3]thiazolo[3,2-a]pyridin-6-yl]carbamate
-
0.1 mM, more than 50% inhibition in extracts from astrocyte-derived cells, extracts from brain-derived endothelial cells and extracts from fibroblasts
benzyl [(3R,7aS)-3-cyano-5-oxohexahydropyrrolo[2,1-b][1,3]oxazol-6-yl]carbamate
-
0.1 mM, 10-50% inhibition in extracts from fibroblasts
benzyl [(3S,6R,7aR)-3-cyano-5-oxohexahydropyrrolo[2,1-b][1,3]thiazol-6-yl]carbamate
-
0.1 mM, 10-50% inhibition in extracts from astrocyte-derived cells and extracts from brain-derived endothelial cells, more than 50% inhibition in extracts from brain-derived endothelial cells
benzyl [(3S,6S,7aR)-3-cyano-5-oxohexahydropyrrolo[2,1-b][1,3]thiazol-6-yl]carbamate
-
0.1 mM, 10-50% inhibition in extracts from astrocyte-derived cells and brain-derived endothelial cells
benzyl [(4S,7S,8aS)-4-cyano-6-oxohexahydro-2H-pyrrolo[2,1-b][1,3]thiazin-7-yl]carbamate
-
0.1 mM, 10-50% inhibition in extracts from fibroblasts
benzyl [2-(2-cyanopiperidin-1-yl)-2-oxoethyl]carbamate
-
0.1 mM, 10-50% inhibition in extracts from brain-derived endothelial cells and extracts from fibroblasts, more than 50% inhibition in extracts from astrocyte-derived cells
benzyl [2-[(2R)-2-cyanopyrrolidin-1-yl]-2-oxoethyl]carbamate
-
0.02 mM, more than 90% inhibition in extracts from brain-derived endothelial cells, extracts from astrocyte-derived cells and extracts from fibroblasts
benzyl [2-[(2S)-2-cyanopyrrolidin-1-yl]-2-oxoethyl]carbamate
-
0.02 mM, more than 90% inhibition in extracts from brain-derived endothelial cells, extracts from astrocyte-derived cells and extracts from fibroblasts
benzyloxycarbonyl-thioprolyl-thioprolinal
-
specific inhibitor of prolyl oligopeptidase
Cbz-Pro-CN
-
0.1 mM, 10-50% inhibition in extracts from brain-derived endothelial cells
Cbz-Pro-NH2
-
0.1 mM, 10-50% inhibition in extracts from astrocyte-derived cells and extracts from fibroblasts
macranganin
-
from Euphorbia fisheriana, specific, noncompetitive, and strong inhibition
methyl (1R,3S,4S,5S)-3-[[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy]-1,4,5-trihydroxycyclohexanecarboxylate
-
92.6% inhibition at 0.5 mM
methyl (3R,6R,7aS)-6-[[(benzyloxy)carbonyl]amino]-5-oxohexahydropyrrolo[2,1-b][1,3]thiazole-3-carboxylate
-
0.1 mM, 10-50% inhibition in extracts from fibroblasts
methyl (3R,6S,7aS)-6-[[(benzyloxy)carbonyl]amino]-5-oxohexahydropyrrolo[2,1-b][1,3]thiazole-3-carboxylate
-
0.1 mM, 10-50% inhibition in extracts from astrocyte-derived cells and extracts from fibroblasts
methyl 1-cinnamoylpyrrolidine-2-carboxylate
-
less than 10% inhibition at 0.5 mM
methyl 2-(cyclohexylamino)-3-[cyclohexyl(formyl)amino]-4-(methylamino)benzoate
-
-
methyl 3-cyclohexyl-4-(cyclohexylamino)-1-methyl-2,3-dihydro-1H-benzimidazole-5-carboxylate
-
-
rugosin E
-
from Euphorbia supina, specific, noncompetitive, and strong inhibition
SUAM 14746
-
i.e. 3-([4-[2-(E)-styrylphenoxy]butanoyl]-L-4-hydroxyprolyl)thiazolidine
tert-butyl [(2S)-3-methyl-1-(1,3-thiazolidin-3-yl)-1-thioxobutan-2-yl]carbamate
-
-
[(1R,2R)-2-phenylcyclopropyl][(2S,3aS,7aS)-2-(1,3-thiazolidin-3-ylcarbonyl)octahydro-1H-indol-1-yl]methanone
-
-
(6S)-1-chloro-3-[(4-fluorobenzyl)oxy]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
-
-
(6S)-1-chloro-3-[(4-fluorobenzyl)oxy]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
-
is co-crystallized within the catalytic site of a human chimeric POP protein which provides a more detailed understanding of how these inhibitors interact with the key residues within the catalytic pocket
benzyl [(3R,6R,7aS)-3-cyano-5-oxohexahydropyrrolo[2,1-b][1,3]thiazol-6-yl]carbamate
-
-
benzyl [(3R,6R,7aS)-3-cyano-5-oxohexahydropyrrolo[2,1-b][1,3]thiazol-6-yl]carbamate
-
0.02 mM, more than 90% inhibition in extracts from brain-derived endothelial cells, extracts from astrocyte-derived cells and extracts from fibroblasts
benzyloxycarbonyl-Pro-prolinal
-
i.e. Z-Pro-Prolinal, inhibition of cytsolic isozyme, but no inhibition of the extracellular isozyme in serum
JTP-4819
-
i.e. (S)-2-[[(S)-2-(hydroxyacetyl)-1-yrrolidinyl]carbonyl]-N-(phenylmethyl)-1-pyrrolidinecarboxamide
JTP-4819
-
used the tight-binding inhibitor JTP-4819 covalently coupled with fluorescein (FJTP) as a tool to study the changes on expression and localization of POP protein
JTP-4819
-
i.e. (S)-2-[[(S)-2-(hydroxyacetyl)-1-pyrrolidinyl]carbonyl]-N(phenylmethyl)-1-pyrrolidinecarboxamide
KYP-2047
-
i.e. 4-phenylbutanoyl-l-prolyl-2(S)-cyanopyrrolidine, highly potent covalent reversible competitive inhibitor
S 17092
-
selective enzyme inhibitor, pharmacodynamics and pharmacokinetics, overview
S-17092
-
i.e. (2S,3aS,7aS)-1-[[(R,R)-2-phenylcyclopropyl]carbonyl]-2-[(thiazolidin-3-yl)carbonyl] octahydro-1H-indole
additional information
-
resistant to: PMSF, thyorphan, E64 and phosphoramidon
-
additional information
-
at least 3 galloyl groups are required for strong inhibition activity by Euphorbiaceae plants, poor inhibition by 1-galloyl glucopyranoside, 1,6-digalloyl glucopyranoside, 2,6-digalloyl glucopyranoside, 2-galloyl galactose, 6-galloyl-1-O-(4-gallate)-glucopyranoside, 6-galloyl-1-O-(phloroglucinol)-glucopyranoside, gallic acid, furosin, anthricin, gomisin A, tigloyl gomisin, 8-C-(glucopyranosyl)-kaempferol, 3-O-galloyl shikimate, 4-O-galloyl shikimate, 3-O-(2-galloyl-glucopyranosyl)-quercetin, quercetin-3-O-glucopyranoside, alpha-viniferin, 5-O-galloylquininc acid, and shizarin, overview
-
additional information
-
no inhibition by lithium, carbamazepime, desipramine, fluoxetine, and olanzapine
-
additional information
-
structure-function relationship of inhibitors, specificity at the P2 and S3 position, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha-synuclein
plus interferon-gamma increases prolyl endopeptidase activity. Lipopolysaccharide, interferon-gamma or alpha-synuclein alone do not significantly upregulate prolyl endopeptidase enzymatic activity
-
interferon-gamma
combination of lipopolysaccharide or interferon-gamma plus interferon-gamma upregulates prolyl endopeptidase enzymatic activity. Lipopolysaccharide, interferon-gamma or alpha-synuclein alone do not significantly upregulate prolyl endopeptidase enzymatic activity
-
lipopolysaccharide
combination of lipopolysaccharide plus interferon-gamma upregulates prolyl endopeptidase enzymatic activity. Lipopolysaccharide, interferon-gamma or alpha-synuclein alone do not significantly upregulate prolyl endopeptidase enzymatic activity
2-mercaptoethanol
-
activation of the cytsolic isozyme, but not of the extracellular isozyme
additional information
-
decrease in enzyme activity in plasma of relapsing remitting multiple sclerose patients
-
additional information
-
increase of cytosolic enzyme activity in clear cell renal cell carcinoma, urothelial carcinoma of the renal pelvis and head and neck squamous cell carcinoma, increase of cytosolic and membrane-bound enzyme activity in colorectal adenomatous polyps
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00065
2-aminobenzoyl-FPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C
0.00074
2-aminobenzoyl-RPPGFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37°C
0.00081
Abz-Gly-L-Phe-L-Arg-L-Pro-L-Phe(NO2)-L-Arg-L-Ala
-
wild type enzyme, at pH 8.0 and 25°C
0.00921
Abz-Gly-L-Phe-L-Arg-L-Pro-L-Phe(NO2)-L-Arg-L-Ala
-
mutant enzyme T202C/T590C, at pH 8.0 and 25°C
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.97
Abz-Gly-L-Phe-L-Arg-L-Pro-L-Phe(NO2)-L-Arg-L-Ala
-
wild type enzyme, at pH 8.0 and 25°C
1.31
Abz-Gly-L-Phe-L-Arg-L-Pro-L-Phe(NO2)-L-Arg-L-Ala
-
mutant enzyme T202C/T590C, at pH 8.0 and 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000001
(2S)-1-[[(2S)-1-(1-oxo-4-phenylbutyl)-2-pyrrolidinyl]carbonyl]-2-pyrrolidinecarbonitrile
pH 7.5, 37°C, recombinant enzyme
0.0002
benzyl [(3R,6R,7aS)-3-cyano-5-oxohexahydropyrrolo[2,1-b][1,3]thiazol-6-yl]carbamate
-
human brain
0.00554
tert-butyl [(2S)-3-methyl-1-(1,3-thiazolidin-3-yl)-1-thioxobutan-2-yl]carbamate
-
human placenta
0.0000015
[(1R,2R)-2-phenylcyclopropyl][(2S,3aS,7aS)-2-(1,3-thiazolidin-3-ylcarbonyl)octahydro-1H-indol-1-yl]methanone
-
-
0.0000022
[(2R)-1-[N-(2,5-dichlorobenzoyl)glycyl]pyrrolidin-2-yl]boronic acid
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0989
(1R,3S,4S,5S)-1,3,4-tris(acetyloxy)-5-([(2E)-3-[3,4-bis(acetyloxy)phenyl]prop-2-enoyl]oxy)cyclohexanecarboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.023
(1R,3S,4S,5S)-3-[[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy]-1,4,5-trihydroxycyclohexanecarboxylic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.0125
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.198
(2E)-3-(3,4-dimethoxyphenyl)prop-2-enoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.028
(2E)-3-[3,4-bis(acetyloxy)phenyl]prop-2-enoic acid
Homo sapiens
-
pH and temperature not specified in the publication
0.000002
(2S,3aS,7aS)-1-[[(1R,2R)-2-phenylcyclopropyl]carbonyl]-2-(1,3-thiazolidin-3-ylcarbonyl)octahydro-1H-indole
Homo sapiens
-
-
0.000034
(3S)-3-(pyrrolidin-1-ylcarbonyl)-6-[[4-(trifluoromethyl)benzyl]oxy]-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.000031
(3S)-6-[(2,4-difluorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.000064
(3S)-6-[(2,5-difluorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.000018
(3S)-6-[(3,4-difluorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.000022
(3S)-6-[(3,5-difluorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.000004
(3S)-6-[(3,5-difluorobenzyl)oxy]-8-(phenylsulfonyl)-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.000022
(3S)-6-[(4-fluorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.00006
(3S)-6-[(4-tert-butylbenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.00027
(3S)-6-[(4-tert-butylbenzyl)oxy]-8-(phenylsulfonyl)-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.000011
(3S)-8-(phenylsulfonyl)-3-(pyrrolidin-1-ylcarbonyl)-6-[[4-(trifluoromethyl)benzyl]oxy]-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.000584
(3S)-8-acetyl-3-(pyrrolidin-1-ylcarbonyl)-6-(2,2,2-trifluoroethoxy)-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.000028
(3S)-8-acetyl-3-(pyrrolidin-1-ylcarbonyl)-6-[[4-(trifluoromethyl)benzyl]oxy]-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.000002
(3S)-8-acetyl-6-(2-phenylethyl)-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.000028
(3S)-8-acetyl-6-[(3,4-dichlorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.000007
(3S)-8-acetyl-6-[(3,4-difluorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.000022
(3S)-8-acetyl-6-[(3,5-difluorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.000008
(3S)-8-acetyl-6-[(3-chloro-4-fluorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.000048
(3S)-8-acetyl-6-[(4-chlorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.000343
(3S)-8-acetyl-6-[(4-fluorobenzyl)oxy]-3-(1H-pyrazol-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.000053
(3S)-8-acetyl-6-[(4-fluorobenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.00014
(3S)-8-acetyl-6-[(4-methoxybenzyl)oxy]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.00003
(3S)-8-acetyl-6-[2-(4-fluorophenyl)ethyl]-3-(pyrrolidin-1-ylcarbonyl)-2,3-dihydroindolizin-5(1H)-one
Homo sapiens
-
-
0.0143
(5R,7S,8S,9S)-8,9-dihydroxy-2,2-dimethyl-4-oxo-1,3-dioxaspiro[4.5]dec-7-yl (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
Homo sapiens
-
pH and temperature not specified in the publication
0.0031
(6S)-1,3-dichloro-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
Homo sapiens
-
-
0.000007
(6S)-1-chloro-3-(cyclohexylmethoxy)-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
Homo sapiens
-
-
0.004
(6S)-1-chloro-3-(naphthalen-2-ylmethoxy)-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
Homo sapiens
-
-
0.0008
(6S)-1-chloro-3-(pyridin-4-ylmethoxy)-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
Homo sapiens
-
-
0.001
(6S)-1-chloro-3-phenoxy-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
Homo sapiens
-
-
0.00008
(6S)-1-chloro-3-[(2-phenylethyl)amino]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
Homo sapiens
-
-
0.000034
(6S)-1-chloro-3-[(3,4-dichlorobenzyl)oxy]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
Homo sapiens
-
-
0.000015
(6S)-1-chloro-3-[(3,4-difluorobenzyl)amino]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
Homo sapiens
-
-
0.000055
(6S)-1-chloro-3-[(3,4-difluorobenzyl)oxy]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
Homo sapiens
-
-
0.000043
(6S)-1-chloro-3-[(3-chloro-4-fluorobenzyl)oxy]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
Homo sapiens
-
-
0.00003
(6S)-1-chloro-3-[(3-chlorobenzyl)oxy]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
Homo sapiens
-
-
0.000017
(6S)-1-chloro-3-[(4-fluorobenzyl)amino]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
Homo sapiens
-
-
0.000012 - 0.00004
(6S)-1-chloro-3-[(4-fluorobenzyl)oxy]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
0.0022
(6S)-1-chloro-3-[2-(3,4-dichlorophenyl)ethoxy]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
Homo sapiens
-
-
0.0009
(6S)-1-chloro-3-[2-(4-fluorophenyl)ethoxy]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
Homo sapiens
-
-
0.00004
(6S)-1-chloro-6-(pyrrolidin-1-ylcarbonyl)-3-[(2,3,5-trifluorobenzyl)oxy]-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
Homo sapiens
-
-
0.00025
(6S)-1-chloro-6-(pyrrolidin-1-ylcarbonyl)-3-[[4-(trifluoromethyl)benzyl]oxy]-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
Homo sapiens
-
-
0.000012
(6S)-3-(benzylamino)-1-chloro-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
Homo sapiens
-
-
0.12
(E)-4-(3-(2-(methoxycarbonyl)pyrrolidin-1-yl)-3-oxoprop-1-enyl)-1,2-phenylene-diacetate
Homo sapiens
-
pH and temperature not specified in the publication
0.1057
(E)-methyl 1-(3-(3,4-dihydroxyphenyl)acryloyl)pyrrolidine-2-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.21
(E)-methyl 1-(3-(3-(3,4-dihydroxyphenyl)acryloyloxy)-1,4,5-trihydroxycyclohexanecarbonyl)pyrrolidine-2-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.00001
(S)-1-((S)-1-(4-phenylbutanoyl)-pyrrolidine-2-carbonyl)pyrrolidine-2-carbonitrile
Homo sapiens
-
in situ assay, pH and temperature not specified in the publication
0.051
1,3-dibenzyl-4-(benzylamino)-5-(methoxycarbonyl)-1H-3,1-benzimidazol-3-ium iodide
Homo sapiens
-
-
0.214
1,3-dicyclohexyl-4-(cyclohexylamino)-5-(methoxycarbonyl)-1H-3,1-benzimidazol-3-ium iodide
Homo sapiens
-
-
0.122
1-benzyl-3-cyclohexyl-4-(cyclohexylamino)-5-(methoxycarbonyl)-1H-3,1-benzimidazol-3-ium iodide
Homo sapiens
-
-
0.037
1-benzyl-3-cyclohexyl-4-(cyclohexylamino)-5-(methoxymethyl)-1H-3,1-benzimidazol-3-ium iodide
Homo sapiens
-
-
0.147
3-benzyl-4-(benzylamino)-5-(methoxycarbonyl)-1-methyl-1H-3,1-benzimidazol-3-ium iodide
Homo sapiens
-
-
0.129
3-cyclohexyl-4-(cyclohexylamino)-1-ethyl-5-[(prop-2-en-1-yloxy)carbonyl]-1H-3,1-benzimidazol-3-ium iodide
Homo sapiens
-
-
0.14
3-cyclohexyl-4-(cyclohexylamino)-1-methyl-5-[(prop-2-en-1-yloxy)carbonyl]-1H-3,1-benzimidazol-3-ium iodide
Homo sapiens
-
-
0.194
3-cyclohexyl-4-(cyclohexylamino)-5-(methoxycarbonyl)-1-(4-methylphenyl)-1H-3,1-benzimidazol-3-ium iodide
Homo sapiens
-
-
0.072
3-cyclohexyl-4-(cyclohexylamino)-5-(methoxycarbonyl)-1-methyl-1H-3,1-benzimidazol-3-ium iodide
Homo sapiens
-
-
0.169
3-cyclohexyl-4-(cyclohexylamino)-5-(methoxycarbonyl)-1-[(1S)-1-phenylethyl]-1H-3,1-benzimidazol-3-ium iodide
Homo sapiens
-
-
0.065 - 0.133
4-(4-chlorophenyl)-8-(ethoxycarbonyl)-5-methyl-2,3-dihydrofuro[3,2-c]quinolin-5-ium iodide
0.000783
4-([[(3S)-8-acetyl-5-oxo-3-(pyrrolidin-1-ylcarbonyl)-1,2,3,5-tetrahydroindolizin-6-yl]oxy]methyl)benzonitrile
Homo sapiens
-
-
0.00055
4-phenyl-1-[(3S)-3-(pyrrolidin-1-ylcarbonyl)-3,4-dihydroisoquinolin-2(1H)-yl]butan-1-one
Homo sapiens
-
-
0.124
5-(4-chlorophenyl)-9-(ethoxycarbonyl)-6-methyl-3,4-dihydro-2H-pyrano[3,2-c]quinolin-6-ium iodide
Homo sapiens
-
-
0.099
5-(methoxycarbonyl)-3-(4-methoxyphenyl)-4-[(4-methoxyphenyl)amino]-1-methyl-1H-3,1-benzimidazol-3-ium iodide
Homo sapiens
-
-
0.201
5-cyano-3-cyclohexyl-4-(cyclohexylamino)-1-methyl-1H-3,1-benzimidazol-3-ium iodide
Homo sapiens
-
-
0.075
8-(ethoxycarbonyl)-5-methyl-4-naphthalen-1-yl-2,3-dihydrofuro[3,2-c]quinolin-5-ium iodide
Homo sapiens
-
-
0.135
9-(ethoxycarbonyl)-6-methyl-5-phenyl-3,4-dihydro-2H-pyrano[3,2-c]quinolin-6-ium iodide
Homo sapiens
-
-
4.9
benzyl (2S)-2-[(2S)-2-formylpyrrolidine-1-carbonyl]pyrrolidine-1-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.014
benzyl (2S)-2-[[(2S)-2-(hydroxymethyl)pyrrolidin-1-yl]carbonyl]pyrrolidine-1-carboxylate
Homo sapiens
-
human peripheral blood mononuclear cells
0.00294
Boc-Asn-Phe-Pro-aldehyde
Homo sapiens
-
in situ assay, pH and temperature not specified in the publication
1
galanthamine
Homo sapiens
-
IC50 above 1.0 mM, pH and temperature not specified in the publication
1
isocorydine
Homo sapiens
-
IC50 above 1.0 mM, pH and temperature not specified in the publication
0.003
methyl (1R,3S,4S,5S)-3-[[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy]-1,4,5-trihydroxycyclohexanecarboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.005
methyl (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
Homo sapiens
-
pH and temperature not specified in the publication
0.005111
Z-Pro-Pro-aldehyde-dimethylacetal
Homo sapiens
-
in situ assay, pH and temperature not specified in the publication
0.000012
(6S)-1-chloro-3-[(4-fluorobenzyl)oxy]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
Homo sapiens
-
-
0.00004
(6S)-1-chloro-3-[(4-fluorobenzyl)oxy]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one
Homo sapiens
-
-
0.065
4-(4-chlorophenyl)-8-(ethoxycarbonyl)-5-methyl-2,3-dihydrofuro[3,2-c]quinolin-5-ium iodide
Homo sapiens
-
-
0.133
4-(4-chlorophenyl)-8-(ethoxycarbonyl)-5-methyl-2,3-dihydrofuro[3,2-c]quinolin-5-ium iodide
Homo sapiens
-
-
0.1354
N-methyllaurotetanine
Homo sapiens
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.066
-
pH 7.4, 22°C, substrate benzyloxycarbonyl-Gly-L-Pro-7-amido-4-methylcoumarin
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
-
reaction with 2-aminobenzoyl-FPQ-(N-(2,4-dinitrophenyl)ethylenediamine), and a second lower optimum at pH 8.0
9
-
reaction with 2-aminobenzoyl-RPPGFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
8
-
reaction with bradykinin. And a second higher optimum at pH 6.5, reaction with 2-aminobenzoyl-FPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
-
pH 7.0: about 55% of maximal activity, pH 9.0: about 30% of maximal activity, reaction with bradykinin
8.5 - 10
-
pH 8.5: about 40% of maximal activity, pH 10.0: about 80% of maximal activity, reaction with 2-aminobenzoyl-BKQRPPGFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
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
additional information
-
highest enzyme activity in the brain cortex, and lowest in the cerebellum
-
of Alzheimer's disease patients, showing high enzyme expression levels, and healthy individuals
additional information
-
no enzyme activity in intestinal brush-border membranes and pancreas
additional information
-
no enzyme in pancreatic/intestinal brush border membranes
additional information
-
the distribution of the enzsm in brain tissue correlates with the distribution of the IP3-receptor
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
additional information
-
the highest levels in particulate fractions in the synaptosomal and the myelin fractions with a a fibrillary, cytoskeleton-like distribution, the enzyme is co-localized with tubulin and is a binding partner of tubulin, overview
-
-
enzyme activity is located only in the cytoplasm during maturation and ageing
-
at an early developmental phase significant amounts are found also in nuclei
-
main localizaztion, enzyme is associated with the microtubulin cytoskeleton. Disruption of microtubules by nocodazole disrupts both the fibrillar tubulin and enzyme labelling
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
prolyl oligopeptidase is a second-step enzyme in the release of acetyl-N-L-Ser-L-Asp-L-Lys-L-Pro from thymosin beta4, and it has autoregulatory effect in the first step
physiological function
additional information
malfunction
-
involvement of enzyme in mechanisms of neoplastic processes suggested
malfunction
-
inhibition or knockdown of prolyl oligopeptidase leads to suppression of NB-1 cell growth, and the effect is accompanied by G0/G1 arrest
malfunction
-
depletion/inhibition of prolylcarboxypeptidase (PRCP)/prolylendopeptidase (PREP) suppresses rapamycin-induced activation of PI3K/AKT with consequent additive/synergistic cytotoxicity
physiological function
-
implicated in neurodegeneration and in modulation of the inflammatory response
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
physiological function
-
prolyl oligopeptidase participates in cell cycle progression in human NB-1 neuroblastoma cells
physiological function
-
prolyl oligopeptidase with thymosin beta4 significantly induces angiogenesis of human umbilical vein endothelial cells. Prolyl oligopeptidase has a pro-angiogenic role via the release of acetyl-N-L-Ser-L-Asp-L-Lys-L-Pro from its precursor thymosin beta4
physiological function
-
PRCP and PREP regulate IRS-1 stability and PI3K/AKT activation in pancreatic cancer
physiological function
-
prolyl oligopeptidase is a glyceraldehyde-3-phosphate dehydrogenase-binding protein that regulates genotoxic stress-induced cell death. Prolyl oligopeptidase mediates glyceraldehyde-3-phosphate dehydrogenase nuclear localization
physiological function
-
the enzyme is associated with secretory processes as well as in reproduction
physiological function
-
increased enzyme levels promote epidermal growth factor receptor signaling, which in turn activates matrix metalloproteinase-9
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_HUMAN
710
0
80700
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
inhibitor (6S)-1-chloro-3-[(4-fluorobenzyl)oxy]-6-(pyrrolidin-1-ylcarbonyl)-7,8-dihydropyrrolo[1,2-a]pyrazin-4(6H)-one is co-crystallized within the catalytic site of a human chimeric POP protein which provides a more detailed understanding of how these inhibitors interact with the key residues within the catalytic pocket
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E289G
-
improved protein stability, 4fold longer half-life at 37°C compared to wild-type
T202C
-
the mutation increases the flexibility of loop A, enhancing the catalytic efficiency 2fold beyond that of the native enzyme
T202C/T590C
-
the mutant shows more than 10fold increased Km and increased kcat values towards Abz-Gly-L-Phe-L-Arg-L-Pro-L-Phe(NO2)-L-Arg-L-Ala at pH 8.0 compared to the wild type enzyme
T590C
-
variant displays an altered substrate preference profile, with reduced ligand binding capacity. The mutation in loop B increased the preference for shorter peptides, indicating a role in substrate gating
additional information
-
enzyme inhibition or enzyme antisense mRNA expression result in enhanced peptide/protein secretion from cells
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
wild-type, 20 min, 15% loss of activity in phosphate-buffered saline, 69% loss of activiy in human serum
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and anion exchange chromatography
ethanol precipitation, Fractogel EMD SO3 chromatography, Blue Sepharose column chromatography, and HA Ultrogel chromatography
-
glutathione Sepharose column chromatography and Mono Q 5/50 GL column chromatography
-
native enzyme expressed in Escherichia coli is rapidly thermally inactivated. Mutation E289G improves protein stability
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene PREP, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cytoplasmic PREP activity decreases slowly and steadily from DIV 0 throughout the growth curve until reaching confluence (between DIV 10 and 15)
-
PREP activity inside the nucleus increases 3fold at DIV 1 compared with its initial levels, PREP nuclearactivity decline dramatically until the cells reach confluence (right after DIV 10)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
inhibition of the enzyme may be a therapeutic approach to neurodegenerative disorders including Alzheimer and Parkinson diseases
drug development
-
the enzyme is a pharmacological target for neurological diseases due to its high brain concentration and ability to cleave neuropeptides in vitro
medicine
medicine
-
enzyme levels in postmortem brains of Alzheimers disease patients reveal significant increases in enzyme activity. Use of unsaturated fatty acids in preventing memory loss
medicine
-
use of enzyme in antibody-directed enzyme prodrug therapy strategy, ADEPT. Coupling of enzyme mutant E289G to human antibody specific to the EDB domain of fibronectin, conjugate retains antigen binding and enzymatic activity
medicine
-
potential target in cognitive function, memory and neurodegenerative disorders
medicine
-
target for the treatment of neuropsychiatric diseases and cognitive disturbances
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mizutani, S.; Sumi, S.; Suzuki, O.; Narita, O.; Tomoda, Y.
Post-proline endopeptidase in human placenta
Biochim. Biophys. Acta
786
113-117
1984
Homo sapiens
Daly, D.J.; Maskrey, P.; Mantle, D.; Pennington, R.J.T.
Proline endopeptidase in human muscle
Biochem. Soc. Trans.
13
1161-1163
1985
Homo sapiens
-
Momand, J.; Clarke, S.
Rapid degradation of D- and L-succinimide-containing peptides by a post-proline endopeptidase from human erythrocytes
Biochemistry
26
7798-7805
1987
Homo sapiens
Goossens, F.; De Meester, I.; Vanhoof, G.; Hendriks, D.; Vriend, G.; Scharpe, S.
The purification, characterization and analysis of primary and secondary-structure of prolyl oligopeptidase from human lymphocytes. Evidence that the enzyme belongs to the alpha/beta hydrolase fold family
Eur. J. Biochem.
233
432-441
1995
Homo sapiens
Shirasawa, Y.; Osawa, T.; Hirashima, A.
Molecular cloning and characterization of prolyl endopeptidase from human T cells
J. Biochem.
115
724-729
1994
Homo sapiens
Quinto, B.M.; Juliano, M.A.; Hirata, I.; Carmona, A.K.; Juliano, L.; Casarini, D.E.
Characterization of a prolyl endopeptidase (kininase) from human urine using fluorogenic quenched substrates
Int. J. Biochem. Cell Biol.
32
1161-1172
2000
Homo sapiens
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
-
Heinis, C.; Alessi, P.; Neri, D.
Engineering a thermostable human prolyl endopeptidase for antibody-directed enzyme prodrug therapy
Biochemistry
43
6293-6303
2004
Homo sapiens
Szeltner, Z.; Alshafee, I.; Juhasz, T.; Parvari, R.; Polgar, L.
The PREPL A protein, a new member of the prolyl oligopeptidase family, lacking catalytic activity
Cell. Mol. Life Sci.
62
2376-2381
2005
Homo sapiens (Q4J6C6)
Park, Y.S.; Jang, H.J.; Lee, K.H.; Hahn, T.R.; Paik, Y.S.
Prolyl endopeptidase inhibitory activity of unsaturated fatty acids
J. Agric. Food Chem.
54
1238-1242
2006
Homo sapiens
Schulz, I.; Zeitschel, U.; Rudolph, T.; Ruiz-Carrillo, D.; Rahfeld, J.U.; Gerhartz, B.; Bigl, V.; Demuth, H.U.; Rossner, S.
Subcellular localization suggests novel functions for prolyl endopeptidase in protein secretion
J. Neurochem.
94
970-979
2005
Homo sapiens
Lee, S.H.; Jun, M.; Choi, J.Y.; Yang, E.J.; Hur, J.M.; Bae, K.; Seong, Y.H.; Huh, T.L.; Song, K.S.
Plant phenolics as prolyl endopeptidase inhibitors
Arch. Pharm. Res.
30
827-833
2007
Homo sapiens
Rea, D.; Fueloep, V.
Structure-function properties of prolyl oligopeptidase family enzymes
Cell Biochem. Biophys.
44
349-365
2006
Homo sapiens, Myxococcus xanthus, Pyrococcus furiosus, Trypanosoma cruzi, Novosphingobium capsulatum (Q9ZNM8)
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
Brandt, I.; Scharpe, S.; Lambeir, A.M.
Suggested functions for prolyl oligopeptidase: a puzzling paradox
Clin. Chim. Acta
377
50-61
2007
Elizabethkingia meningoseptica, Homo sapiens, Mus musculus, Rattus norvegicus, Trypanosoma cruzi
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
Myoehaenen, T.T.; Venaelaeinen, J.I.; Tupala, E.; Garcia-Horsman, J.A.; Miettinen, R.; Maennistoe, P.T.
Distribution of immunoreactive prolyl oligopeptidase in human and rat brain
Neurochem. Res.
32
1365-1374
2007
Homo sapiens, Rattus norvegicus
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)
Haffner, C.D.; Diaz, C.J.; Miller, A.B.; Reid, R.A.; Madauss, K.P.; Hassell, A.; Hanlon, M.H.; Porter, D.J.; Becherer, J.D.; Carter, L.H.
Pyrrolidinyl pyridone and pyrazinone analogues as potent inhibitors of prolyl oligopeptidase (POP)
Bioorg. Med. Chem. Lett.
18
4360-4363
2008
Homo sapiens
Tarrago, T.; Masdeu, C.; Gomez, E.; Isambert, N.; Lavilla, R.; Giralt, E.
Benzimidazolium salts as small, nonpeptidic and BBB-permeable human prolyl oligopeptidase inhibitors
ChemMedChem
3
1558-1565
2008
Homo sapiens
Klegeris, A.; Li, J.; Bammler, T.K.; Jin, J.; Zhu, D.; Kashima, D.T.; Pan, S.; Hashioka, S.; Maguire, J.; McGeer, P.L.; Zhang, J.
Prolyl endopeptidase is revealed following SILAC analysis to be a novel mediator of human microglial and THP-1 cell neurotoxicity
Glia
56
675-685
2008
Homo sapiens (P48147)
Van Gool, A.R.; Verkerk, R.; Fekkes, D.; Sleijfer, S.; Bannink, M.; Kruit, W.H.; van der Holt, B.; Scharpe, S.; Eggermont, A.M.; Stoter, G.; Hengeveld, M.W.
Plasma activity of prolyl endopeptidase in relation to psychopathology during immunotherapy with IFN-alpha in patients with renal cell carcinoma
J. Interferon Cytokine Res.
28
283-286
2008
Homo sapiens
Moreno-Baylach, M.J.; Felipo, V.; Maennistoe, P.T.; Garcia-Horsman, J.A.
Expression and traffic of cellular prolyl oligopeptidase are regulated during cerebellar granule cell differentiation, maturation, and aging
Neuroscience
156
580-585
2008
Homo sapiens
Tarrago, T.; Martin-Benito, J.; Sabido, E.; Claasen, B.; Madurga, S.; Gairi, M.; Valpuesta, J.M.; Giralt, E.
A new side opening on prolyl oligopeptidase revealed by electron microscopy
FEBS Lett.
583
3344-3348
2009
Homo sapiens
Marques, M.R.; Stueker, C.; Kichik, N.; Tarrago, T.; Giralt, E.; Morel, A.F.; Dalcol, I.I.
Flavonoids with prolyl oligopeptidase inhibitory activity isolated from Scutellaria racemosa Pers
Fitoterapia
81
552-6
2010
Homo sapiens
Lawandi, J.; Toumieux, S.; Seyer, V.; Campbell, P.; Thielges, S.; Juillerat-Jeanneret, L.; Moitessier, N.
Constrained peptidomimetics reveal detailed geometric requirements of covalent prolyl oligopeptidase inhibitors
J. Med. Chem.
52
6672-6684
2009
Homo sapiens
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)
OReilly, P.J.; Hardison, M.T.; Jackson, P.L.; Xu, X.; Snelgrove, R.J.; Gaggar, A.; Galin, F.S.; Blalock, J.E.
Neutrophils contain prolyl endopeptidase and generate the chemotactic peptide, PGP, from collagen
J. Neuroimmunol.
217
51-54
2009
Homo sapiens
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
Larrinaga, G.; Perez, I.; Blanco, L.; Lopez, J.I.; Andres, L.; Etxezarraga, C.; Santaolalla, F.; Zabala, A.; Varona, A.; Irazusta, J.
Increased prolyl endopeptidase activity in human neoplasia
Regul. Pept.
163
102-106
2010
Homo sapiens
Sakaguchi, M.; Matsuda, T.; Matsumura, E.; Yoshimoto, T.; Takaoka, M.
Prolyl oligopeptidase participates in cell cycle progression in a human neuroblastoma cell line
Biochem. Biophys. Res. Commun.
409
693-698
2011
Homo sapiens
Myoehaenen, T.T.; Tenorio-Laranga, J.; Jokinen, B.; Vazquez-Sanchez, R.; Moreno-Baylach, M.J.; Garcia-Horsman, J.A.; Maennistoe, P.T.
Prolyl oligopeptidase induces angiogenesis both in vitro and in vivo in a novel regulatory manner
Br. J. Pharmacol.
163
1666-1678
2011
Homo sapiens, Rattus norvegicus
Huang, C.H.; Suen, C.S.; Lin, C.T.; Chien, C.H.; Lee, H.Y.; Chung, K.M.; Tsai, T.Y.; Jiaang, W.T.; Hwang, M.J.; Chen, X.
Cleavage-site specificity of prolyl endopeptidase FAP investigated with a full-length protein substrate
J. Biochem.
149
685-692
2011
Homo sapiens
Klimaviciusa, L.; Jain, R.K.; Jaako, K.; Van Elzen, R.; Gerard, M.; van Der Veken, P.; Lambeir, A.M.; Zharkovsky, A.
In situ prolyl oligopeptidase activity assay in neural cell cultures
J. Neurosci. Methods
204
104-110
2012
Homo sapiens, Rattus norvegicus
Moreno-Baylach, M.J.; Puttonen, K.A.; Tenorio-Laranga, J.; Venaelaeinen, J.I.; Storvik, M.; Forsberg, M.M.; Garcia-Horsman, J.A.
Prolyl endopeptidase is involved in cellular signalling in human neuroblastoma SH-SY5Y cells
Neurosignals
19
97-109
2011
Homo sapiens
Szeltner, Z.; Juhasz, T.; Szamosi, I.; Rea, D.; Fueloep, V.; Modos, K.; Juliano, L.; Polgar, L.
The loops facing the active site of prolyl oligopeptidase are crucial components in substrate gating and specificity
Biochim. Biophys. Acta
1834
98-111
2013
Homo sapiens
Rentzsch, A.; Kahlert, V.; Jahreis, G.; Schlott, B.; Schutkowski, M.; Malesevic, M.; Fischer, G.
Identification of prolyl oligopeptidase as a cyclosporine-sensitive protease by screening of mouse liver extracts
Biol. Chem.
394
1057-1067
2013
Homo sapiens
Jambunathan, K.; Watson, D.S.; Endsley, A.N.; Kodukula, K.; Galande, A.K.
Comparative analysis of the substrate preferences of two post-proline cleaving endopeptidases, prolyl oligopeptidase and fibroblast activation protein alpha
FEBS Lett.
586
2507-2512
2012
Homo sapiens
Matsuda, T.; Sakaguchi, M.; Tanaka, S.; Yoshimoto, T.; Takaoka, M.
Prolyl oligopeptidase is a glyceraldehyde-3-phosphate dehydrogenase-binding protein that regulates genotoxic stress-induced cell death
Int. J. Biochem. Cell Biol.
45
850-857
2013
Homo sapiens
Duan, L.; Ying, G.; Danzer, B.; Perez, R.E.; Shariat-Madar, Z.; Levenson, V.V.; Maki, C.G.
The prolyl peptidases PRCP/PREP regulate IRS-1 stability critical for rapamycin-induced feedback activation of PI3K and AKT
J. Biol. Chem.
289
21694-21705
2014
Homo sapiens
Myoehaenen, T.T.; Pyykkoe, E.; Maennistoe, P.T.; Carpen, O.
Distribution of prolyl oligopeptidase in human peripheral tissues and in ovarian and colorectal tumors
J. Histochem. Cytochem.
60
706-715
2012
Homo sapiens
Poplawski, S.E.; Lai, J.H.; Li, Y.; Jin, Z.; Liu, Y.; Wu, W.; Wu, Y.; Zhou, Y.; Sudmeier, J.L.; Sanford, D.G.; Bachovchin, W.W.
Identification of selective and potent inhibitors of fibroblast activation protein and prolyl oligopeptidase
J. Med. Chem.
56
3467-3477
2013
Homo sapiens
Hannula, M.J.; Myoehaenen, T.T.; Tenorio-Laranga, J.; Maennistoe, P.T.; Garcia-Horsman, J.A.
Prolyl oligopeptidase colocalizes with alpha-synuclein, beta-amyloid, tau protein and astroglia in the post-mortem brain samples with Parkinsons and Alzheimers diseases
Neuroscience
242
140-150
2013
Homo sapiens
Adolpho, L.O.; Marin, D.; Puigpinos, A.; Mendieta, L.; Tarrago, T.; Morel, A.F.; Giralt, E.; Dalcol, I.I.
In vitro evaluation of caffeoyl and cinnamoyl derivatives as potential prolyl oligopeptidase inhibitors
Planta Med.
79
1531-1535
2013
Homo sapiens
Lopez, A.; Herranz-Trillo, F.; Kotev, M.; Gairi, M.; Guallar, V.; Bernado, P.; Millet, O.; Tarrago, T.; Giralt, E.
Active-site-directed inhibitors of prolyl oligopeptidase abolish its conformational dynamics
ChemBioChem
17
913-917
2016
Homo sapiens
Cahlikova, L.; Hulova, L.; Hrabinova, M.; Chlebek, J.; Hostalkova, A.; Adamcova, M.; Safratova, M.; Jun, D.; Opletal, L.; Locarek, M.; Macakova, K.
Isoquinoline alkaloids as prolyl oligopeptidase inhibitors
Fitoterapia
103
192-196
2015
Homo sapiens
Jaako, K.; Waniek, A.; Parik, K.; Klimaviciusa, L.; Aonurm-Helm, A.; Noortoots, A.; Anier, K.; Van Elzen, R.; Gerard, M.; Lambeir, A.M.; Rossner, S.; Morawski, M.; Zharkovsky, A.
Prolyl endopeptidase is involved in the degradation of neural cell adhesion molecules in vitro
J. Cell Sci.
129
3792-3802
2016
Homo sapiens
Hostalkova, A.; Opletal, L.; Kunes, J.; Novak, Z.; Hrabinova, M.; Chlebek, J.; Cegan, L.; Cahlikova, L.
Alkaloids from Peumus boldus and their acetylcholinesterase, butyrylcholinesterase and prolyl oligopeptidase inhibition activity
Nat. Prod. Commun.
10
577-580
2015
Homo sapiens
Fajtova, P.; Stefanic, S.; Hradilek, M.; Dvorak, J.; Vondrasek, J.; Jilkova, A.; Ulrychova, L.; McKerrow, J.H.; Caffrey, C.R.; Mares, M.; Horn, M.
Prolyl oligopeptidase from the blood fluke Schistosoma mansoni From functional analysis to anti-schistosomal inhibitors
PLoS Negl. Trop. Dis.
9
e0003827
2015
Homo sapiens, Schistosoma mansoni (W8GKU3), Schistosoma mansoni
EXTERNAL LINKS (specific for EC-Number 3.4.21.26)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
