Information on EC 3.4.21.26 - prolyl oligopeptidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
3.4.21.26
-
RECOMMENDED NAME
GeneOntology No.
prolyl oligopeptidase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
show the reaction diagram
-
-
-
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
show the reaction diagram
catalytic triad consists of Ser548-Asp631-His667
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
the catalytic triad is formed by conserved residues Ser548, Asp631, and His667
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
show the reaction diagram
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
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
show the reaction diagram
catalytic residues are Ser477, Asp559, and His591
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
show the reaction diagram
catalytic mechanism, structure-function relationship
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
show the reaction diagram
catalytic mechanism, structure-function relationship, the substrate induces an opening at the interface pf the peptidase and the beta-propeller domains while entering into the active site, concerted movements of the domains are required for enzyme activity
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
show the reaction diagram
catalytic mechanism, structure-function relationship
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
-
-
hydrolysis of peptide bond
-
-
endopeptidase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cyproase I
-
engineered proline-specific endopeptidase
endoprolylpeptidase
-
-
-
-
fibroblast activation protein
-
-
mPOP
-
-
PEP
Aspergillus oryzae WX2011
-
-
-
peptidase, postproline endo-
-
-
-
-
post proline cleaving enzyme
-
-
post prolyl cleaving enzyme
-
-
post-proline cleaving endopeptidase
-
-
post-proline cleaving enzyme
-
-
-
-
post-proline cleaving enzyme
-
-
post-proline cleaving enzyme
-
-
post-proline cleaving enzyme
-
-
post-proline cutting enzyme
-
-
post-proline endopeptidase
-
-
-
-
post-proline endopeptidase
-
-
post-proline endopeptidase
-
post-proline endopeptidase
-
-
postproline cleaving enzyme
-
postproline endopeptidase
-
-
-
-
postproline-cleaving enzyme
-
-
-
-
PPCE
-
-
PREP
-
-
proline endopeptidase
-
-
-
-
proline-specific endopeptidase
-
-
-
-
proline-specific endopeptidase
-
-
proly endopeptidase
-
-
prolyl endopeptidase
-
-
-
-
prolyl endopeptidase
-
prolyl endopeptidase
-
-
prolyl endopeptidase
Aspergillus oryzae WX2011
-
-
-
prolyl endopeptidase
-
-
prolyl endopeptidase
-
-
prolyl endopeptidase
-
-
prolyl endopeptidase
-
-
prolyl endopeptidase
-
-
prolyl endopeptidase
-
-
prolyl endopeptidase
-
prolyl endopeptidase
-
-
prolyl endopeptidase
-
prolyl endoprotease
-
-
prolyl endoprotease
-
prolyl endoprotease
-
-
prolyl oligopeptidase
-
-
prolyl oligopeptidase
-
-
prolyl oligopeptidase
-
prolyl oligopeptidase
-
-
prolyl oligopeptidase
-
-
prolyl oligopeptidase
-
-
prolyl oligopeptidase
-
-
prolyl oligopeptidase
-
prolyl oligopeptidase
-
-
prolyl oligopeptidase
-
prolyl oligopeptidase
-
prolylendopeptidase
-
-
prolylendopeptidase
-
-
prost-proline cleaving enzyme
-
-
membrane-bound PE
-
-
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
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 serine peptidase family with post-proline cleaving activity towards peptides
additional information
-
the enzyme is a member of the prolyl oligopeptidase family, subfamily S9a
CAS REGISTRY NUMBER
COMMENTARY
72162-84-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform POPA
UniProt
Manually annotated by BRENDA team
isoform POPB
UniProt
Manually annotated by BRENDA team
ATC29413
-
-
Manually annotated by BRENDA team
Anabaena variabilis ATC29413
ATC29413
-
-
Manually annotated by BRENDA team
Columbia ecotype
-
-
Manually annotated by BRENDA team
Ascidia sp.
-
-
-
Manually annotated by BRENDA team
Aspergillus oryzae WX2011
-
-
-
Manually annotated by BRENDA team
estimated as a fraction of papaya latex
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
2 isoenzymes
-
-
Manually annotated by BRENDA team
female and male Caucasian individuals
-
-
Manually annotated by BRENDA team
gene prep
-
-
Manually annotated by BRENDA team
patients with Alzheimers disease
-
-
Manually annotated by BRENDA team
recombinant enzyme
-
-
Manually annotated by BRENDA team
splice variant PREPL A lacking peptidase activity
SwissProt
Manually annotated by BRENDA team
Barbara ecotype
-
-
Manually annotated by BRENDA team
Lyophyllum cinerascens
-
-
-
Manually annotated by BRENDA team
gene prep
-
-
Manually annotated by BRENDA team
male animal
-
-
Manually annotated by BRENDA team
male NMRI mice
-
-
Manually annotated by BRENDA team
male Swiss strain mice
-
-
Manually annotated by BRENDA team
mice with a gene-trap of prolyl endopeptidase
-
-
Manually annotated by BRENDA team
Pseudomonas sp. KU-22
KU-22
-
-
Manually annotated by BRENDA team
young, male Wistar rats
-
-
Manually annotated by BRENDA team
flesh fly
-
-
Manually annotated by BRENDA team
strain NA1, isolated from the deep-sea hydrohermal vent area of the PACMANUS field in the East Manus Basin
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
enzyme associated with schizophrenia, bipolar affective disorder and related neuropsychiatric disorders
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
metabolism
-
prolyl endopeptidase is involved in collagen breakdown
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
-
regulation of the brain levels of biologically active peptide substrates and phosphatidylinosital system, influence on memory and mood, possible role in motor functions
physiological function
-
involved in memory-related function
physiological function
-
regulates appetite or milk production
physiological function
-
important function in learning and memory processes, psychological disorders and neurodegenerative diseases
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
-
implicated in neurodegeneration and in modulation of the inflammatory response
physiological function
important role in host interactions
physiological function
-
cigarette smoke-induced lung emphysema in mice is associated with prolyl endopeptidase
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
-
prolyl oligopeptidase has a pro-angiogenic role via the release of acetyl-N-Ser-Asp-Lys-Pro from its precursor thymosin beta4
physiological function
-
the enzyme is implicated in neuropeptide processing
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
-
PRCP and PREP regulate IRS-1 stability and PI3K/AKT activation in pancreatic cancer
physiological function
-
the enzyme is associated with secretory processes as well as in reproduction
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-benzyl 2-(2-(4-hydroxynaphthalen-1-ylcarbamoyl)pyrrolidin-1-yl)-2-oxoethylcarbamate + H2O
?
show the reaction diagram
-
specific substrate, UAMC-00682
-
-
?
18 kD protein of photosystem II + H2O
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
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
show the reaction diagram
-
the fluorescence resonance energy transfer peptide sequence corresponds to bradykinin from human kininogen
-
?
2-aminobenzoyl-EGPQGLLGA-3-nitrotyrosyl-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-FFQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-FPQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
2-aminobenzoyl-FP + Q-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
2-aminobenzoyl-FSQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
?
2-aminobenzoyl-Glu-Gly-Phe-Ser-Pro-Phe(NO2)-Arg-Ala + H2O
2-aminobenzoyl-Glu-Gly-Phe-Ser-Pro + Phe(NO2)-Arg-Ala
show the reaction diagram
-
-
-
?
2-aminobenzoyl-Glu-Phe-Ser-Pro-Phe(NO2)-Arg-Ala + H2O
2-aminobenzoyl-Glu-Phe-Ser-Pro + Phe(NO2)-Arg-Ala
show the reaction diagram
-
-
-
?
2-aminobenzoyl-Gly-Glu-Ser-Pro-Phe(NO2)-Arg-Ala + H2O
2-aminobenzoyl-Gly-Glu-Ser-Pro + Phe(NO2)-Arg-Ala
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
2-aminobenzoyl-Gly-Phe-Arg-Pro-Phe(NO2)-Arg-Ala + H2O
2-aminobenzoyl-Gly-Phe-Arg-Pro + Phe(NO2)-Arg-Ala
show the reaction diagram
-
-
-
?
2-aminobenzoyl-Gly-Phe-Glu-Pro-Phe(NO2)-Arg-Ala + H2O
2-aminobenzoyl-Gly-Phe-Glu-Pro + Phe(NO2)-Arg-Ala
show the reaction diagram
-
-
-
?
2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
the enzyme binds no more than six residues, P4-P2' even from a longer substrate
-
?
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
a fluorescence resonance energy transfer peptide, the fluorescence resonance energy transfer peptide sequence corresponds to bradykinin from human kininogen
-
?
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
a fluorescence resonance energy transfer peptide
-
?
2-aminobenzoyl-L-Ser-L-Pro-L-4-nitrophenylalanine-L-Ala + H2O
2-aminobenzoyl-L-Ser-L-Pro + 4-nitrophenylalanine-L-Ala
show the reaction diagram
-
-
-
?
2-aminobenzoyl-RPPGFQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
show the reaction diagram
-
-
-
-
?
2-aminobenzoyl-RPPGFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
2-aminobenzoyl-RPP + GFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
show the reaction diagram
-
-
-
?
2-aminobenzoyl-SPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine) + H2O
?
show the reaction diagram
-
-
-
-
?
4-((4-(dimethylamino)phenyl)azo)benzoyl-GPQGLLGA-L-glutamyl-gamma-(2-(1-sulfonyl-5-naphthyl)-aminoethylamide)-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
-
?
AbzGFGPFGF(p-NO2)A-NH2 + H2O
AbzGFGP + HN2-FGF(p-NO2)A-NH2
show the reaction diagram
-
assay at pH 8.0, 37C, reaction stopped by heating at 95C for 5 min
-
?
Ac-CDPGYIGSR-NH2 + H2O
?
show the reaction diagram
-
substrate specificity studies on membrane PE as compared with POP. ZPP-sensitive cleavage of both occurred
-
-
?
Ala-Ala-Pro-4-nitroanilide + H2O
Ala-Ala-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
?
Ala-Gly-Pro-beta-naphthylamide + H2O
Ala-Gly-Pro + beta-naphthylamide
show the reaction diagram
Lyophyllum cinerascens
-
-
-
?
Ala-Pro-4-nitroanilide + H2O
Ala-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
?
Ala-Pro-p-nitroanilide + H2O
Ala-Pro + p-nitroaniline
show the reaction diagram
-
-
-
?
alpa2-antiplasmin + H2O
?
show the reaction diagram
-
not a robust substrate in vitro, the enzyme cleaves after Pro12 in the T9S10G11P12-N13 Q14E15Q16E17 sequence
-
-
?
alpha-melanocyte-stimulating hormone + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-melanocyte-stimulating hormone + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-melanocyte-stimulating hormone + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-melanocyte-stimulating hormone + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-MSH(1-13) + H2O
alpha-MSH(1-12) + Pro
show the reaction diagram
-
increased ratio between substrate and product in pituitaries of prolyl endopeptidase deficient mice compared to wild type mice
-
?
alpha-synuclein + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-synulein + H2O
?
show the reaction diagram
-
the enzyme binds to alpha-synuclein and enhances its dimerization
-
-
?
alpha2-gliadin 33-mer + H2O
?
show the reaction diagram
-
the enzyme is able to break down 63% of the 33-mer after 8 h of incubation and it is almost completely degraded after 12 h
-
-
?
Angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
-
Angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
Angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
Angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
Angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
Angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
Angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
Angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
Angiotensin II + H2O
?
show the reaction diagram
-
-
-
-
?
Angiotensin II + H2O
?
show the reaction diagram
-
-
-
-
?
Angiotensin II + H2O
?
show the reaction diagram
-
-
-
-
?
Arg-Pro-4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
?
Arg-Pro-Lys-His-Pro-Ile-Lys-His-Gln + H2O
Arg-Pro-Lys-His-Pro + Ile-Lys-His-Gln
show the reaction diagram
i.e. alphaS1-casein(1-9), cleavage at Pro5-Ile6
-
?
Arg-Pro-p-nitroanilide + H2O
Arg-Pro + p-nitroaniline
show the reaction diagram
-
-
-
?
arginine-vasopressin + H2O
?
show the reaction diagram
-
-
-
-
?
arginine-vasopressin + H2O
?
show the reaction diagram
-
-
-
-
?
arginine-vasopressin + H2O
?
show the reaction diagram
-
-
-
-
?
arginine-vasopressin + H2O
?
show the reaction diagram
-
-
-
-
?
Asp-Pro-4-nitroanilide + H2O
Asp-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
?
Asp-Pro-p-nitroanilide + H2O
Asp-Pro + p-nitroaniline
show the reaction diagram
-
-
-
?
azocasein + H2O
?
show the reaction diagram
-
-
-
-
?
azocasein + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
benzoyloxycarbonyl-Gly-L-Pro-Nap + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ala-Ala-4-nitroanilide + H2O
benzyloxycarbonyl-Ala-Ala + 4-nitroaniline
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Ala-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Ala + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Ala-p-nitroanilide + H2O
benzyloxycarbonyl-Ala-Ala + p-nitroaniline
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Ala-p-nitrophenol + H2O
benzyloxycarbonyl-Ala-Ala + p-nitrophenol
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Gly-Pro + beta-naphthylamine
show the reaction diagram
Elizabethkingia meningoseptica, Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Ala-Gly-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Ala-Gly-Pro + p-nitrophenol
show the reaction diagram
-
enzyme from kidney
-
?
benzyloxycarbonyl-Ala-Pro-2-naphthylamide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ala-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Ala-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Ala-Pro + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Pro-p-nitroanilide + H2O
benzyloxycarbonyl-Ala-Pro + p-nitroaniline
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Pro-p-nitroanilide + H2O
benzyloxycarbonyl-Ala-Pro + p-nitroaniline
show the reaction diagram
Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Ala-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Ala-Pro + p-nitrophenol
show the reaction diagram
-
enzyme from kidney
-
?
benzyloxycarbonyl-D-Ala-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-D-Ala-Gly-Pro + beta-naphthylamine
show the reaction diagram
Elizabethkingia meningoseptica, Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-D-Ala-Gly-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-D-Ala-Gly-Pro + p-nitrophenol
show the reaction diagram
-
enzyme from kidney
-
?
benzyloxycarbonyl-D-Ala-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-D-Ala-Pro + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Gly-Gly-Pro + p-nitrophenol
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Gly-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Gly-Gly-Pro + p-nitrophenol
show the reaction diagram
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-L-Pro-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-L-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-L-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-L-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-L-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gly-L-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-beta-naphthylamide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-doxorubicin + H2O
benzyloxycarbonyl-Gly-L-Pro + doxorubicin
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-L-Pro-melphalan + H2O
benzyloxycarbonyl-Gly-L-Pro + melphalan
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Pro-2-beta-naphthylamide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-2-beta-naphthylamide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-2-beta-naphthylamide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-2-beta-naphthylamide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-2-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + 2-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Pro-2-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + 2-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Pro-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-4-methylcoumaryl-7-amide + H2O
benzyloxycarbonyl-Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
Elizabethkingia meningoseptica, Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Gly-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-Gly-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Pro-4-nitrophenyl ester + H2O
benzyloxycarbonyl-Gly-Pro + 4-nitrophenol
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Ala
show the reaction diagram
Elizabethkingia meningoseptica, Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Ala
show the reaction diagram
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + beta-naphthylamine
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + beta-naphthylamide
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + beta-naphthylamide
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Pro-D-Ala + H2O
benzyloxycarbonyl-Gly-Pro + D-Ala
show the reaction diagram
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-D-Leu + H2O
benzyloxycarbonyl-Gly-Pro + D-Leu
show the reaction diagram
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-Leu + H2O
benzyloxycarbonyl-Gly-Pro + Leu
show the reaction diagram
Elizabethkingia meningoseptica, Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu + H2O
benzyloxycarbonyl-Gly-Pro + Leu
show the reaction diagram
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Ala
show the reaction diagram
Elizabethkingia meningoseptica, Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Ala
show the reaction diagram
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-Leu-D-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Leu-D-Ala
show the reaction diagram
Elizabethkingia meningoseptica, Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu-D-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Leu-D-Ala
show the reaction diagram
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Gly
show the reaction diagram
Elizabethkingia meningoseptica, Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Gly
show the reaction diagram
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Gly-Ala
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Gly-Ala
show the reaction diagram
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly-D-Ala + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Gly-D-Ala
show the reaction diagram
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Gly + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Gly-Gly
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Gly + H2O
benzyloxycarbonyl-Gly-Pro + Leu-Gly-Gly
show the reaction diagram
-
enzyme from kidney
-
?
Benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro + H2O
Benzyloxycarbonyl-Gly-Pro + Leu-Gly-Pro
show the reaction diagram
Lyophyllum cinerascens
-
-
-
?
Benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro + H2O
Benzyloxycarbonyl-Gly-Pro + Leu-Gly-Pro
show the reaction diagram
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-p-nitroanilide + H2O
benzyloxycarbonyl-Gly-Pro + p-nitroaniline
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Pro-p-nitroanilide + H2O
benzyloxycarbonyl-Gly-Pro + p-nitroaniline
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Pro-p-nitroanilide + H2O
benzyloxycarbonyl-Gly-Pro + p-nitroaniline
show the reaction diagram
Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Gly-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Gly-Pro + p-nitrophenol
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Gly-Pro + p-nitrophenol
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Gly-Pro + p-nitrophenol
show the reaction diagram
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-Phe + H2O
benzyloxycarbonyl-Gly-Pro + Phe
show the reaction diagram
Elizabethkingia meningoseptica, Lyophyllum cinerascens
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Phe + H2O
benzyloxycarbonyl-Gly-Pro + Phe
show the reaction diagram
-
enzyme from kidney
-
?
benzyloxycarbonyl-Gly-Pro-SBzl + H2O
benzyloxycarbonyl-Gly-Pro + phenyl-methanethiol
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Gly-Pro-thiobenzyl ester + H2O
benzyloxycarbonyl-Gly-Pro + phenylmethanethiol
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-glycyl-l-prolyl-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-glycyl-proline-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-glycyl-proline-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-glycyl-proline-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-glycyl-proline-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-glycyl-proline-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-glycyl-proline-p-nitroanilide + H2O
?
show the reaction diagram
Anabaena variabilis ATC29413
-
-
-
-
?
benzyloxycarbonyl-L-Ala-L-Ala-L-Pro p-nitroanilide + H2O
?
show the reaction diagram
Pseudomonas sp., Pseudomonas sp. KU-22
-
-
-
-
?
benzyloxycarbonyl-Pro-p-nitrophenol + H2O
benzyloxycarbonyl-Pro + p-nitrophenol
show the reaction diagram
-
enzyme from kidney
-
?
beta-amyloid + H2O
?
show the reaction diagram
-
-
-
-
?
beta-endorphin + H2O
?
show the reaction diagram
-
-
-
-
?
beta-endorphin + H2O
?
show the reaction diagram
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
-
-
?
calcitonin gene-related peptide + H2O
?
show the reaction diagram
-
assay at pH 7.0, 37C
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
the pathogen POP degrades host collagen and fibronectin, facilitating cell invasion, selective inhibitors for trypanosome POP block parasite entry into cells, host-derived substrate
-
-
?
collagen + H2O
N-acetyl-Pro-Gly-Pro + ?
show the reaction diagram
-
after enzyme activation with LPS
-
?
collagen + H2O
Pro-Gly-Pro + ?
show the reaction diagram
-
after enzyme activation with LPS
-
?
collagen I + H2O
?
show the reaction diagram
assay at pH 8.0, 37C
-
-
?
collagens + H2O
?
show the reaction diagram
-
in host extracellular matrix, mammalian substrate
-
-
?
DRVYIHPF + H2O
DRVYIHP + L-Phe
show the reaction diagram
-
-
-
?
EYYDPNYLRT + H2O
EYDP + NYLRT
show the reaction diagram
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
in host extracellular matrix
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
the pathogen POP degrades host collagen and fibronectin, facilitating cell invasion, selective inhibitors for trypanosome POP block parasite entry into cells, host-derived substrate
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
mammalian substrate
-
-
?
furylacryloyl-Ala-Pro + H2O
?
show the reaction diagram
-
-
-
-
?
FVNEHLCGSHLVQALTLVCGQRGFFYTPLA + H2O
FVNEHLCGSHLVQALTLVCGQRGFFYTP + LA
show the reaction diagram
-
-
-
?
GEPGPPGPA + H2O
GEP + GPPGP + L-Ala
show the reaction diagram
-
-
-
?
GFSPFRQED + H2O
GFSP + FRQED
show the reaction diagram
-
-
-
?
gliadins + H2O
?
show the reaction diagram
-
in host gut, mammalian substrate
-
-
?
gluten + H2O
?
show the reaction diagram
-
-
-
-
?
gluten + H2O
?
show the reaction diagram
-
-
-
-
?
gluten + H2O
?
show the reaction diagram
-
-
-
-
?
gluten + H2O
?
show the reaction diagram
-
-
-
-
?
gluten + H2O
?
show the reaction diagram
-
-
-
-
?
gluten + H2O
?
show the reaction diagram
-
-
-
-
?
gluten + H2O
?
show the reaction diagram
-
activity in the human host gastrointestinal tract, overview
-
-
?
gluten + H2O
?
show the reaction diagram
-
degradation of gluten in the human host's intestinal tract, i.e. stomach, duodenum, jejunum, and ileum, determination of activity in a dynamic system that closely mimics the human gastrointestinal tract, overview
-
-
?
gluten peptides + H2O
?
show the reaction diagram
-
activity in the human host gastrointestinal tract, overview
-
-
?
gluten peptides + H2O
?
show the reaction diagram
-
degradation of gluten peptides in the human host's intestinal tract, i.e. stomach, duodenum, jejunum, and ileum, determination of activity in a dynamic system that closely mimics the human gastrointestinal tract, overview
-
-
?
Gly-L-Pro-4-nitroanilide + H2O
Gly-L-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
?
Gly-L-Pro-4-nitroanilide + H2O
Gly-L-Pro + 4-nitroaniline
show the reaction diagram
-
-
?
Gly-L-Pro-7-amido-4-methylcoumarin + H2O
Gly-L-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Gly-Pro-4-methoxy-beta-naphthylamide + H2O
Gly-Pro + 4-methoxy-beta-naphthylamine
show the reaction diagram
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
show the reaction diagram
-
-
-
?
GnRH + H2O
?
show the reaction diagram
-
-
-
?
gonadotropin releasing hormone + H2O
?
show the reaction diagram
-
-
-
-
?
gonadotropin releasing hormone + H2O
?
show the reaction diagram
-
-
-
-
?
gonadotropin releasing hormone + H2O
?
show the reaction diagram
-
-
-
-
?
gonadotropin releasing hormone + H2O
?
show the reaction diagram
-
-
-
-
?
GTAGPNQEQE + H2O
GTAGP + NQEQE
show the reaction diagram
-
-
-
?
GTSGPNQEQE + H2O
GTSGP + NQEQE
show the reaction diagram
-
-
-
?
H-(O2Oc)2-K(Abz)GFGPFGF(p-NO2)A-NH2 + H2O
?
show the reaction diagram
-
assay at pH 8.0, 37C, reaction stopped by heating at 95C for 5 min
-
-
?
H-Abz-GFGP-OH + H2O
?
show the reaction diagram
-
assay at pH 8.0, 37C, reaction stopped by heating at 95C for 5 min
-
-
?
H-Abz-GFGPFGF(p-NO2)A-NH2 + H2O
?
show the reaction diagram
-
assay at pH 8.0, 37C, reaction stopped by heating at 95C for 5 min
-
-
?
H-F(p-NO2)GFGP-OH + H2O
?
show the reaction diagram
-
assay at pH 8.0, 37C, reaction stopped by heating at 95C 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
show the reaction diagram
-
assay at pH 8.0, 37C, reaction stopped by heating at 95C for 5 min
-
?
H-F(p-NO2)GFGPFGK(Abz)A-(O2Oc)-NH2 + H2O
H-F(p-NO2)GFGP + FGK(Abz)A-(O2Oc)-NH2
show the reaction diagram
-
assay at pH 8.0, 37C, reaction stopped by heating at 95C 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
show the reaction diagram
-
assay at pH 8.0, 37C, reaction stopped by heating at 95C 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
show the reaction diagram
-
assay at pH 8.0, 37C, reaction stopped by heating at 95C for 5 min
-
?
H-F(p-NO2)GFGPFGK(Abz)A-HMBA-PEGA + H2O
H-F(p-NO2)GFGP + FGK(Abz)A-HMBA-PEGA
show the reaction diagram
-
assay at pH 8.0, 37C, reaction stopped by heating at 95C for 5 min
-
?
H-F(p-NO2)GFGPFGK(Abz)A-NH2 + H2O
H-F(p-NO2)GFGP + FGK(Abz)A-NH2
show the reaction diagram
-
assay at pH 8.0, 37C, reaction stopped by heating at 95C for 5 min
-
?
H-FGF(p-NO2)A-NH2 + H2O
?
show the reaction diagram
-
assay at pH 8.0, 37C, reaction stopped by heating at 95C for 5 min
-
-
?
H-K(Abz)-GFGPFGF(p-NO2)A-NH2 + H2O
?
show the reaction diagram
-
assay at pH 8.0, 37C, reaction stopped by heating at 95C for 5 min
-
-
?
H-MDPVDPNIE-OH + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
assay at pH 8.0, 37C, reaction stopped by heating at 95C for 5 min
-
-
?
H2N-QLQPFPQPQLPY-OH + H2O
?
show the reaction diagram
-
substrate specificity studies on membrane PE as compared with POP. ZPP-sensitive cleavage of both occurred
-
-
?
hemoglobin beta-chain + H2O
?
show the reaction diagram
-
-
-
-
?
insulin + H2O
?
show the reaction diagram
-
-
-
-
?
insulin + H2O
?
show the reaction diagram
-
-
-
-
?
ISRPPGFSPFR + H2O
ISRPP + GFSPFR
show the reaction diagram
-
-
-
?
L-Ala-L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala-L-Ala-L-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
?
L-Ala-L-Ala-L-Pro-4-nitroanilide + H2O
L-Ala-L-Ala-L-Pro + 4-nitroaniline
show the reaction diagram
Aspergillus oryzae, Aspergillus oryzae WX2011
-
-
-
?
LVVYPWTQRF + H2O
LVVYP + WTQRF
show the reaction diagram
-
prolyl endopeptidase activity could be the first step of the degradation of LVV-hemorphin-7
-
?
Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Lys-Arg-Pro-Pro + Gly-Phe-Ser-Pro-Phe-Arg
show the reaction diagram
-
as active as potentiator B
-
?
Me-O-succinyl-Ala-Ala-Val p-nitroanilide + H2O
Me-O-succinyl-Ala-Ala + Val p-nitroanilide
show the reaction diagram
-
-
-
?
N-benzoyl-L-Phe-L-Val-L-Arg-4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-Ala-Ala-p-nitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Pro-p-nitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-carbobenzoxy-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
N-carbobenzoxy-Gly-L-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-carbobenzoxy-Gly-Pro-7-amido-4-methyl-coumarin + H2O
?
show the reaction diagram
-
-
-
-
?
N-carbobenzyloxy-Ala-Pro-2-naphthylamide + H2O
N-carbobenzyloxy-Ala-Pro + 2-naphthylamine
show the reaction diagram
-
-
-
?
N-carbobenzyloxy-glycyl-proline-4-methyloumarin-7-amide + H2O
N-carbobenzyloxy-glycyl-proline + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-Suc-Ala-Ala-Ala-7-amido-4-methylcoumarin + H2O
N-Suc-Ala-Ala-Ala + 7-amino-4-methylcoumarin
show the reaction diagram
assay at pH 7.5, 25C
-
?
N-Suc-Gly-Pro-7-amido-4-methylcoumarin + H2O
N-Suc-Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
assay at pH 7.5, 25C
-
?
N-Suc-Gly-Pro-Leu-Gly-Pro-7-amido-4-methylcoumarin + H2O
N-Suc-Gly-Pro-Leu-Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
assay at pH 7.5, 25C
-
?
N-succinyl-Ala-Ala-Ala-4-nitroanilide
N-succinyl-Ala-Ala-Ala + 4-nitroaniline
show the reaction diagram
-
-
-
-
N-succinyl-Ala-Pro-4-nitroanilide + H2O
N-succinyl-Ala-Pro + 4-nitroaniline
show the reaction diagram
-
-
?
N-succinyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
24% of the activity with N-succinyl-Gly-L-Pro-L-Leu-Gly-L-Pro-7-amido-4-methylcoumarin
-
-
?
N-succinyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
N-succinyl-Gly-L-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-succinyl-Gly-L-Pro-L-Leu-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
?
N-succinyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
N-succinyl-Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-succinyl-Gly-Pro-OH + H2O
?
show the reaction diagram
-
-
-
-
?
N-succinyl-glycyl-proline-4-methylcoumarin-7-amide + H2O
N-succinyl-glycyl-proline + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-succinyl-glycyl-prolyl-7-amido-4-methylcoumarin + H2O
N-succinyl-glycyl-prolyl + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-succinyl-glycyl-prolyl-7-amido-4-methylcoumarin + H2O
N-succinyl-glycyl-prolyl + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-succinyl-glycyl-prolyl-7-amido-4-methylcoumarin + H2O
N-succinyl-glycyl-prolyl + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
N-succinyl-L-Ala-L-Ala-L-Ala-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
13% of the activity with N-succinyl-Gly-L-Pro-L-Leu-Gly-L-Pro-7-amido-4-methylcoumarin
-
-
?
Nalpha-benzyl-Gly-Pro-Leu-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-Gly-Pro-Leu-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzyloxycarbonyl-Gly-Pro-Leu-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
?
oxytocin + H2O
inactivated oxytocin + dipeptide
show the reaction diagram
-
-
-
?
oxytocin + H2O
?
show the reaction diagram
-
-
-
-
?
PEGA(O2Oc)2-K(Abz)GFGPFGF(p-NO2)A-NH2 + H2O
?
show the reaction diagram
-
assay at pH 8.0, 37C, reaction stopped by heating at 95C for 5 min
-
-
?
PEGA-K(ABz)-GFGPFGF(p-NO2)A-NH2 + H2O
?
show the reaction diagram
-
assay at pH 8.0, 37C, reaction stopped by heating at 95C for 5 min
-
-
?
PEGA-O2Oc-K(Abz)GFGPFGF(p-NO2)A-NH2 + H2O
?
show the reaction diagram
-
assay at pH 8.0, 37C, reaction stopped by heating at 95C for 5 min
-
-
?
peptide QATVGDVNTDRPGLLDLK + H2O
TVGDVNTDRPGLLDLK + GDVNTDRPGLLDLK + QA + QATV
show the reaction diagram
-
i.e. octadecaneuropeptide ODN, the biologically active fragment of diazepam-binding inhibitor, the Ala2 residue is preferred by the enzyme for cleavage, while the Pro-Gly bind is not cleaved, overview
-
?
Peptides + H2O
?
show the reaction diagram
-
involved in process of fertilization, between chorion elevation and cell cleavage
-
-
-
Peptides + H2O
?
show the reaction diagram
-
metabolism of peptides containing altered aspartyl residues
-
-
-
pGlu-Gly-Leu-Pro-Pro-Arg-Pro + H2O
pGlu-Gly-Leu-Pro-Pro + Arg-Pro
show the reaction diagram
-
i.e. potentiator B
-
?
pGlu-Gly-Leu-Pro-Pro-Gly-Pro + H2O
pGlu-Gly-Leu-Pro-Pro + Gly-Pro
show the reaction diagram
-
i.e. potentiator C, as active as potentiator B
-
?
RPKPQQFFGLM + H2O
L-Arg-L-Pro + L-Lys-L-Pro + QQFFGLM
show the reaction diagram
-
-
-
?
RPPGFSPFR + H2O
?
show the reaction diagram
-
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
show the reaction diagram
-
i.e. bradykinin, 70% of the activity with potentiator B, i.e. pGlu-Gly-Leu-Pro-Pro-Arg-Pro
-
?
somatostatin-28 (1-12) + H2O
?
show the reaction diagram
-
-
-
-
?
SPRY2 + H2O
?
show the reaction diagram
-
not an in vivo substrate of fibroblast activation protein
-
-
?
Substance P + H2O
?
show the reaction diagram
-
-
-
-
?
Substance P + H2O
?
show the reaction diagram
-
-
-
-
?
Substance P + H2O
?
show the reaction diagram
-
-
-
-
?
Substance P + H2O
?
show the reaction diagram
-
-
-
-
?
Suc-Gly-Pro-7-amino-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Ala-Pro-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-D-Ala-Pro-4-nitroanilide + H2O
benzyloxycarbonyl-D-Ala-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
?
succinyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
succinyl-Gly-L-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
succinyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
succinyl-Gly-L-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
succinyl-Gly-Pro-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Gly-Pro-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Gly-Pro-4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Gly-Pro-4-methylcoumaryl-7-amide + H2O
succinyl-Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
succinyl-Gly-Pro-4-methylcoumaryl-7-amide + H2O
succinyl-Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
succinyl-Gly-Pro-4-methylcoumaryl-7-amide + H2O
succinyl-Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
succinyl-Gly-Pro-4-methylcoumaryl-7-amide + H2O
succinyl-Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
succinyl-Gly-Pro-7-amido-4-methylcoumarin + H2O
succinyl-Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
succinyl-Gly-Pro-Leu-Gly-Pro-4-methylcoumaryl-7-amide
?
show the reaction diagram
-
-
-
-
?
succinyl-Gly-Pro-Leu-Gly-Pro-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
tasidotin + H2O
tert-butylamine + ?
show the reaction diagram
-
assay at pH 6.8, 37C
-
?
tau protein + H2O
?
show the reaction diagram
-
-
-
-
?
tert-butyloxycarbonyl-Ala-Ala p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
tert-butyloxycarbonyl-Ala-Ala-Pro-Ala p-nitroanilide + H2O
tert-butyloxycarbonyl-Ala-Ala-Pro + Ala + p-nitoaniline
show the reaction diagram
-
-
-
?
thymosin beta4 + H2O
acetyl-N-L-Ser-L-Asp-L-Lys-L-Pro + ?
show the reaction diagram
-
-
-
?
thymosin beta4 + H2O
acetyl-N-Ser-Asp-Lys-Pro + ?
show the reaction diagram
-
prolyl oligopeptidase is a second-step enzyme in the release of acetyl-N-Ser-Asp-Lys-Pro from thymosin beta4 and has autoregulatory effect in the first step
-
?
thyroliberin + H2O
?
show the reaction diagram
-
-
-
-
?
thyrotropin releasing hormone + H2O
?
show the reaction diagram
-
-
-
-
?
thyrotropin-releasing hormone + H2O
?
show the reaction diagram
-
-
-
-
?
tuftsin + H2O
?
show the reaction diagram
-
-
-
-
?
Tyr-Gln-Glu-Pro-Val-Leu-Gly-Pro-Val-Arg-Gly-Pro-Phe-Pro-Ile-Ile-Val-p-nitroanilide + H2O
?
show the reaction diagram
i.e. N-acetyl-beta-casein-(f203-209)-p-nitroanilide, cleavage at: Pro196-Val197, Pro200-Val201 and Pro206-Ile207
-
-
?
urotensin II + H2O
?
show the reaction diagram
-
human substrate, cleavage at the canonical post-proline site
-
-
?
Vasopressin + H2O
?
show the reaction diagram
-
-
-
-
?
vasopressin + H2O
inactivated vasopressin + dipeptide
show the reaction diagram
-
-
-
?
VHLTPVGL + H2O
VHLTP + VGL
show the reaction diagram
-
-
-
?
Z-Gly-L-Pro-4-nitroanilide + H2O
Z-Gly-L-Pro + 4-nitroaniline
show the reaction diagram
-
-
?
Z-Gly-L-Pro-4-nitroanilide + H2O
Z-Gly-L-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
?
Z-Gly-L-Pro-4-nitroanilide + H2O
Z-Gly-L-Pro + 4-nitroaniline
show the reaction diagram
Aspergillus oryzae, Aspergillus oryzae WX2011
-
-
-
?
Z-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
Z-Gly-L-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Z-Gly-Pro-2-naphthylamide + H2O
Z-Gly-Pro + 2-naphthylamine
show the reaction diagram
-
-
-
?
Z-Gly-Pro-2-naphthylamide + H2O
Z-Gly-Pro + 2-naphthylamine
show the reaction diagram
-
-
-
?
Z-Gly-Pro-4-nitroanilide + H2O
4-nitroaniline + Z-Gly-Pro
show the reaction diagram
-
pH 7.0, room temperature
-
?
Z-Gly-Pro-4-nitroanilide + H2O
Z-Gly-Pro + p-nitroaniline
show the reaction diagram
-
assay at 37C
-
?
Z-Gly-Pro-4-nitroanilide + H2O
Z-Gly-Pro + p-nitroaniline
show the reaction diagram
assay at 37C
-
-
Z-Gly-Pro-4-nitroanilide + H2O
Z-Gly-Pro + p-nitroaniline
show the reaction diagram
assay at pH 5.0, 37C
-
?
Z-Gly-Pro-4-nitroanilide + H2O
Z-Gly-Pro + p-nitroaniline
show the reaction diagram
assay at pH 8.0, 34C
-
?
Z-Gly-Pro-4-nitroanilide + H2O
Z-Gly-Pro + p-nitroaniline
show the reaction diagram
-
chromogenic assay, assay at pH 7.0, 37C, reaction stopped by addition of sodium acetate
-
?
Z-Gly-Pro-4-nitroanilide + H2O
Z-glycyl-L-proline + 4-nitroaniline
show the reaction diagram
-
assay at pH 7.0, 30C
-
?
Z-Gly-Pro-7-amido-4-methylcoumarin
Z-Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
assay at pH 7.0, 30C
-
?
Z-Gly-Pro-7-amido-4-methylcoumarin
Z-Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
assay at pH 8.0, 37C, reaction stopped with sodium acetate
-
-
Z-Gly-Pro-7-amido-4-methylcoumarin
Z-Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
fluorogenic assay, assay at pH 6.8, 37C, reaction stopped by addition of acetic acid
-
?
Z-Gly-Pro-7-amido-4-methylcoumarin + H2O
z-Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Z-Gly-Pro-7-amido-4-methylcoumarin + H2O
z-Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
?
Z-Gly-Pro-7-amido-4-methylcoumarin + H2O
z-Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
assay at pH 7.0, 37C
-
?
Z-Gly-Pro-7-amido-4-methylcoumarin + H2O
z-Gly-Pro + 7-amino-4-methylcoumarin
show the reaction diagram
-
assay at pH 7.0, 30C
-
?
Z-Gly-Pro-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
-
-
-
-
?
Z-Gly-Pro-p-nitroanilide + H2O
Z-Gly-Pro + p-nitroaniline
show the reaction diagram
-
-
-
?
Z-L-Ala-L-Ala-L-Ala-L-Pro-4-nitroanilide + H2O
Z-L-Ala-L-Ala-L-Ala-L-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
?
Z-L-Ala-L-Ala-L-Ala-L-Pro-4-nitroanilide + H2O
Z-L-Ala-L-Ala-L-Ala-L-Pro + 4-nitroaniline
show the reaction diagram
Aspergillus oryzae, Aspergillus oryzae WX2011
-
-
-
?
Met-Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
Met-Lys-Arg-Pro-Pro + Gly-Phe-Ser-Pro-Phe-Arg
show the reaction diagram
-
as active as potentiator B
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
requirement for a trans peptide bond immediately preceding the active bond
-
-
-
additional information
?
-
-
cleavage of Pro-X bond
-
-
-
additional information
?
-
-
cleavage of Pro-X bond, and more slowly Ala-X bond
-
-
-
additional information
?
-
-
succinyl and isoaspartyl containing
-
-
-
additional information
?
-
-
not: (7-D-Pro)oxytocin and high molecular weight proteins even after denaturation
-
-
-
additional information
?
-
-
substrate specificity, overview
-
-
-
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
?
-
-
no hydrolysis of benzyloxycarbonyl-D-Pro-p-nitrophenol, negligibly small hydrolysis rate with benzyloxycarbonyl-D-Ala-Pro-p-nitrophenol
-
-
?
additional information
?
-
-
no hydrolysis of Pro-beta-naphthylamide, benzyloxycarbonyl-Pro-beta-naphthylamide, benzyloxycarbonyl-Ala-p-nitrophenol, Gly-Prp-beta-naphthylamide, Ala-Ala-beta-naphthylamide, benzyloxycarbonyl-Gly-Pro-D-Ala
-
-
?
additional information
?
-
Lyophyllum cinerascens
-
no hydrolysis of Pro-beta-naphthylamide, benzyloxycarbonyl-Pro-beta-naphthylamide, Gly-Pro-beta-naphthylamide, benzyloxycarbonyl-Gly-D-Pro-p-nitroanilide, benzyloxycarbonyl-D-Ala-Pro-beta-naphthylamide and benzyloxycarbonyl-Gly-Pro-D-Ala
-
-
?
additional information
?
-
-
specifically hydrolyzes Pro-Xaa bonds, exerts a low specificity towards residues in position P1', except for Glu and P2 and does not cleave the proline bonds in long substrates such as ribonuclease
-
-
?
additional information
?
-
-
the enzyme plays a role in the metabolism of proline-containing neuropeptides which have been suggested to be involved in learning and memory processes
-
-
?
additional information
?
-
the specificity for post-proline bonds suggests that the enzyme may play a central role in the hydrolysis of casein-derived bitter peptides, such as beta-casein(f193-209)
-
-
?
additional information
?
-
-
tissue-dependent peptide hydrolysis evoked by prolyl endopeptidase activity is involved in the water-electrolyte homeostasis
-
-
?
additional information
?
-
-
enzyme regulation, overview
-
-
-
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
?
-
substrates require a proline in position P1, with the exception of N-succinyl-L-Ala-L-Ala-L-Ala-7-amino-4-methylcoumarin
-
-
-
additional information
?
-
-
cellular functions, overview
-
-
-
additional information
?
-
-
cellular functions, overview, POP may regulate phosphoinositide signaling, overview
-
-
-
additional information
?
-
-
cellular functions, overview, POP may regulate phosphoinositide signaling, overview, the enzyme is involved in Alzheimer's disease with enzyme inhibition leading to a reduction of beta-amyloid peptide, overview
-
-
-
additional information
?
-
-
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
?
-
-
enzyme inhibition leads to inhibition of lithium effects, the loss of enzyme activity evokes a 4fold increase in the inositol-3-phosphate concentration counteracting the Li+ ions, enzyme regulation, overview
-
-
-
additional information
?
-
-
enzyme inhibitors are able to prevent the in vitro invasion of rodent muscle cells by trypomastigotes
-
-
-
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 in the brain dopaminergix system is involved in the pathogenesis of doamine deficiency-dependent depressive states, and is activated in association with development of MPTP-induced depressive syndrome in the brain frontal cortex, overview
-
-
-
additional information
?
-
-
the enzyme induces cleavage of gluten-derived peptides predigested by pepsin and pancreatic enzymes an exhibiting a detoxifying effect in the host's gut
-
-
-
additional information
?
-
-
the enzyme is a proline-specific endopeptidase with a serine-type mechanism
-
-
-
additional information
?
-
-
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 a serine protease, that digests small peptide-like hormones, neuroactive peptides, and various cellular factors, it is implicated in several biological processes and diseases, e.g. in some psychiatric disorders, most probably through interference in the inositol cycle, it is important in the metabolism of substance P, arginine vasopressin, thyroliberin, and gonadoliberin, enzyme regulation, overview
-
-
-
additional information
?
-
-
the enzyme is associated with cognitive functions and inositol 1,4,5-triphosphate signaling, and plays a role in modifying neuropeptide levels, overview
-
-
-
additional information
?
-
-
the enzyme is involved in the phosphoinositide pathway, in formation and processing of amyloid beta-peptide, protein secretion, and in neuronal differentiation and maturation, overview, the enzyme is involved in several diseases, e.g. celiac disease, Alzheimer's diease, Parkinsons's disease, affective disorders, eating disorders, cancer, inflammation, hypertension, and neurodegenarative disorders, overview, enzyme inhibition can improve the retention time when administered before either the acquisition or the retential trial in scopolamine-induced amnesia, enzyme inhibition also positively affects neurodiseases, overview
-
-
-
additional information
?
-
-
the enzyme is involved in the phosphoinositide pathway, in formation and processing of amyloid beta-peptide, protein secretion, and in neuronal differentiation and maturation, overview, the enzyme is involved in several diseases, e.g. celiac disease, Alzheimer's diease, Parkinsons's disease, affective disorders, eating disorders, cancer, inflammation, hypertension, and neurodegenarative disorders, overview, enzyme inhibition can improve the retention time when administered before either the acquisition or the retential trial in scopolamine-induced amnesia, enzyme inhibition positively affects neurodiseases, overview
-
-
-
additional information
?
-
-
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
-
-
-
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
?
-
-
the enzyme removes most of the gut-digestion-resistant gliadin peptides in the host gut luman of coeliac disease patients, overview, enzyme regulation, overview
-
-
-
additional information
?
-
-
no activity with gluten in celiac sprue patients, substrate specificity with exclusion of peptides with more than 30 amino acids, overview
-
-
-
additional information
?
-
-
no activity with gluten in celiac sprue rats, substrate specificity with exclusion of peptides with more than 30 amino acids, overview
-
-
-
additional information
?
-
-
POP is a proline-specific peptidase that hydrolyzes oligopeptides after prolyl residues, the S1 binding site of POP has evolved to fit the pyrrolidine ring of an L-prolyl residue
-
-
-
additional information
?
-
-
substrate specificity 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
?
-
-
substrate specificity, overview, the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, the S2' subsite had the highest specificity of the S1'-S3' subsites, this subsite prefers Pro residues, followed by Leu, Met, Phe, and Ala residues, the S1' subsite has lower specificity than the S2', with the strongest preference for hydrophobic, e.g. Leu, and aromatic, e.g. Phe, residues, and the greatest discrimination against Pro residues
-
-
-
additional information
?
-
-
the enzyme cleaves at the C-terminal side of proline residues, the bacterial enzyme is also capable of cleaving Ala-Xaa and Val-Xaa bonds, no activity with large proteins with over 30 amino acids
-
-
-
additional information
?
-
-
the enzyme cleaves the peptide bond on the C-terminal side of proline in peptides up to approx 30 residues, and hydrolyse several peptide hormones and neuropeptides in vitro
-
-
-
additional information
?
-
-
the enzyme cleaves the peptide bond on the C-terminal side of proline in peptides up to approx 30 residues, substrate entry into the active site cavity, substrate-binding structure and mechanism, general acid/base catalysis is the rate-limiting step, overview
-
-
-
additional information
?
-
-
the enzyme cleaves the peptide bond on the C-terminal side of proline in peptides up to approx 30 residues, substrate entry into the active site cavity, substrate-binding structure and mechanism, overview
-
-
-
additional information
?
-
the enzyme cleaves the peptide bond on the C-terminal side of proline in peptides up to approx 30 residues, substrate entry into the active site cavity, substrate-binding structure and mechanism, the loops connecting the peptidase and propeller domains act like a hinge, holding the structure together as the domains move apart, creating a large opening, overview
-
-
-
additional information
?
-
-
the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, substrate specificity, overview
-
-
-
additional information
?
-
-
the enzyme shows endopeptidase activity with peptides no longer than 3 amino acids
-
-
-
additional information
?
-
-
the enzyme shows endopeptidase activity with peptides no longer than 30 amino acids
-
-
-
additional information
?
-
-
the serine protease cleaves at the C-terminal side of proline residues and more slowly of alanine residues of peptides with no more than 30 amino acids
-
-
-
additional information
?
-
-
ability to cleave immunotoxic gluten peptides endoproteolytically, attractive oral therapeutic candidates for protecting celiac sprue patients from the toxic effects of dietary gluten
-
-
-
additional information
?
-
-
cleaves short proline-containing neuropeptides, and is involved in memory and learning
-
-
-
additional information
?
-
-
hydrolyzes proline-containing peptides shorter than 30 amino acids
-
-
-
additional information
?
-
-
is involved in thalamocortical and corticothalamic signal processing
-
-
-
additional information
?
-
prolyl oligopeptidase binds to the growth-38 associated protein GAP-43, which is a key regulator of synaptic plasticity
-
-
-
additional information
?
-
-
stimulates the aggregation of alpha-synuclein
-
-
-
additional information
?
-
-
leginsulin appears to be a possible candidate for the POP substrate
-
-
-
additional information
?
-
-
substance P, arginine-vasopressin, thyroliberin and gonadoliberin are proposed physiological substrates of this protease. No ZPP-sensitive cleavage occurred with the 33-mer, PEP-3, PEP-26, PEP-48_2, and PEP-50
-
-
-
additional information
?
-
-
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
?
-
-
the recombinant prolyl oligopeptidase is not able to cleave whole 43-mer thymosin beta4, while it is effective at hydrolyzing somatostatin-28 (1-12)
-
-
-
additional information
?
-
-
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
?
-
-
does not cleave GASGPAGPA
-
-
-
additional information
?
-
-
no activity toward L-Pro-4-nitroanilide, Gly-L-Pro-4-nitroanilide, Z-Pro-nitrophenyl ester, Z-Gly-Gly-nitrophenyl ester, Z-Phe-Arg-7-amido-4-methylcoumarin, Z-Leu-Leu-Glu-7-amido-4-methylcoumarin, Z-Val-Lys-Met-7-amido-4-methylcoumarin, Z-Leu-Leu-Leu-7-amido-4-methylcoumarin, and Z-Tyr-Val-Ala-Asp-4-nitroanilide
-
-
-
additional information
?
-
the specificity for post-proline bonds suggests that the enzyme may play a central role in the hydrolysis of casein-derived bitter peptides, such as beta-casein(f193-209)
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpa2-antiplasmin + H2O
?
show the reaction diagram
-
not a robust substrate in vitro, the enzyme cleaves after Pro12 in the T9S10G11P12-N13 Q14E15Q16E17 sequence
-
-
?
alpha-melanocyte-stimulating hormone + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-melanocyte-stimulating hormone + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-melanocyte-stimulating hormone + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-melanocyte-stimulating hormone + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-synuclein + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-synulein + H2O
?
show the reaction diagram
-
the enzyme binds to alpha-synuclein and enhances its dimerization
-
-
?
Angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
Angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
Angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
Angiotensin I + H2O
?
show the reaction diagram
-
-
-
-
?
Angiotensin II + H2O
?
show the reaction diagram
-
-
-
-
?
arginine-vasopressin + H2O
?
show the reaction diagram
-
-
-
-
?
arginine-vasopressin + H2O
?
show the reaction diagram
-
-
-
-
?
arginine-vasopressin + H2O
?
show the reaction diagram
-
-
-
-
?
arginine-vasopressin + H2O
?
show the reaction diagram
-
-
-
-
?
beta-amyloid + H2O
?
show the reaction diagram
-
-
-
-
?
beta-endorphin + H2O
?
show the reaction diagram
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
Bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
the pathogen POP degrades host collagen and fibronectin, facilitating cell invasion, selective inhibitors for trypanosome POP block parasite entry into cells
-
-
?
collagens + H2O
?
show the reaction diagram
-
in host extracellular matrix
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
in host extracellular matrix
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
the pathogen POP degrades host collagen and fibronectin, facilitating cell invasion, selective inhibitors for trypanosome POP block parasite entry into cells
-
-
?
gliadins + H2O
?
show the reaction diagram
-
in host gut
-
-
?
gluten + H2O
?
show the reaction diagram
-
-
-
-
?
gluten + H2O
?
show the reaction diagram
-
activity in the human host gastrointestinal tract, overview
-
-
?
gluten + H2O
?
show the reaction diagram
-
degradation of gluten in the human host's intestinal tract, i.e. stomach, duodenum, jejunum, and ileum
-
-
?
gluten peptides + H2O
?
show the reaction diagram
-
activity in the human host gastrointestinal tract, overview
-
-
?
gluten peptides + H2O
?
show the reaction diagram
-
degradation of gluten peptides in the human host's intestinal tract, i.e. stomach, duodenum, jejunum, and ileum
-
-
?
gonadotropin releasing hormone + H2O
?
show the reaction diagram
-
-
-
-
?
gonadotropin releasing hormone + H2O
?
show the reaction diagram
-
-
-
-
?
gonadotropin releasing hormone + H2O
?
show the reaction diagram
-
-
-
-
?
gonadotropin releasing hormone + H2O
?
show the reaction diagram
-
-
-
-
?
LVVYPWTQRF + H2O
LVVYP + WTQRF
show the reaction diagram
-
prolyl endopeptidase activity could be the first step of the degradation of LVV-hemorphin-7
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
neurotensin + H2O
?
show the reaction diagram
-
-
-
-
?
Peptides + H2O
?
show the reaction diagram
-
involved in process of fertilization, between chorion elevation and cell cleavage
-
-
-
Peptides + H2O
?
show the reaction diagram
-
metabolism of peptides containing altered aspartyl residues
-
-
-
Substance P + H2O
?
show the reaction diagram
-
-
-
-
?
Substance P + H2O
?
show the reaction diagram
-
-
-
-
?
Substance P + H2O
?
show the reaction diagram
-
-
-
-
?
Substance P + H2O
?
show the reaction diagram
-
-
-
-
?
tau protein + H2O
?
show the reaction diagram
-
-
-
-
?
thymosin beta4 + H2O
acetyl-N-L-Ser-L-Asp-L-Lys-L-Pro + ?
show the reaction diagram
-
-
-
?
thyrotropin releasing hormone + H2O
?
show the reaction diagram
-
-
-
-
?
urotensin II + H2O
?
show the reaction diagram
-
human substrate, cleavage at the canonical post-proline site
-
-
?
additional information
?
-
-
the enzyme plays a role in the metabolism of proline-containing neuropeptides which have been suggested to be involved in learning and memory processes
-
-
?
additional information
?
-
Q8VTS9
the specificity for post-proline bonds suggests that the enzyme may play a central role in the hydrolysis of casein-derived bitter peptides, such as beta-casein(f193-209)
-
-
?
additional information
?
-
-
tissue-dependent peptide hydrolysis evoked by prolyl endopeptidase activity is involved in the water-electrolyte homeostasis
-
-
?
additional information
?
-
-
enzyme regulation, overview
-
-
-
additional information
?
-
-
cellular functions, overview
-
-
-
additional information
?
-
-
cellular functions, overview, POP may regulate phosphoinositide signaling, overview
-
-
-
additional information
?
-
-
cellular functions, overview, POP may regulate phosphoinositide signaling, overview, the enzyme is involved in Alzheimer's disease with enzyme inhibition leading to a reduction of beta-amyloid peptide, overview
-
-
-
additional information
?
-
-
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
?
-
-
enzyme inhibition leads to inhibition of lithium effects, the loss of enzyme activity evokes a 4fold increase in the inositol-3-phosphate concentration counteracting the Li+ ions, enzyme regulation, overview
-
-
-
additional information
?
-
-
enzyme inhibitors are able to prevent the in vitro invasion of rodent muscle cells by trypomastigotes
-
-
-
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 in the brain dopaminergix system is involved in the pathogenesis of doamine deficiency-dependent depressive states, and is activated in association with development of MPTP-induced depressive syndrome in the brain frontal cortex, overview
-
-
-
additional information
?
-
-
the enzyme induces cleavage of gluten-derived peptides predigested by pepsin and pancreatic enzymes an exhibiting a detoxifying effect in the host's gut
-
-
-
additional information
?
-
-
the enzyme is a proline-specific endopeptidase with a serine-type mechanism
-
-
-
additional information
?
-
-
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 a serine protease, that digests small peptide-like hormones, neuroactive peptides, and various cellular factors, it is implicated in several biological processes and diseases, e.g. in some psychiatric disorders, most probably through interference in the inositol cycle, it is important in the metabolism of substance P, arginine vasopressin, thyroliberin, and gonadoliberin, enzyme regulation, overview
-
-
-
additional information
?
-
-
the enzyme is associated with cognitive functions and inositol 1,4,5-triphosphate signaling, and plays a role in modifying neuropeptide levels, overview
-
-
-
additional information
?
-
-
the enzyme is involved in the phosphoinositide pathway, in formation and processing of amyloid beta-peptide, protein secretion, and in neuronal differentiation and maturation, overview, the enzyme is involved in several diseases, e.g. celiac disease, Alzheimer's diease, Parkinsons's disease, affective disorders, eating disorders, cancer, inflammation, hypertension, and neurodegenarative disorders, overview, enzyme inhibition can improve the retention time when administered before either the acquisition or the retential trial in scopolamine-induced amnesia, enzyme inhibition also positively affects neurodiseases, overview
-
-
-
additional information
?
-
-
the enzyme is involved in the phosphoinositide pathway, in formation and processing of amyloid beta-peptide, protein secretion, and in neuronal differentiation and maturation, overview, the enzyme is involved in several diseases, e.g. celiac disease, Alzheimer's diease, Parkinsons's disease, affective disorders, eating disorders, cancer, inflammation, hypertension, and neurodegenarative disorders, overview, enzyme inhibition can improve the retention time when administered before either the acquisition or the retential trial in scopolamine-induced amnesia, enzyme inhibition positively affects neurodiseases, overview
-
-
-
additional information
?
-
-
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
-
-
-
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
?
-
-
the enzyme removes most of the gut-digestion-resistant gliadin peptides in the host gut luman of coeliac disease patients, overview, enzyme regulation, overview
-
-
-
additional information
?
-
-
ability to cleave immunotoxic gluten peptides endoproteolytically, attractive oral therapeutic candidates for protecting celiac sprue patients from the toxic effects of dietary gluten
-
-
-
additional information
?
-
-
cleaves short proline-containing neuropeptides, and is involved in memory and learning
-
-
-
additional information
?
-
-
hydrolyzes proline-containing peptides shorter than 30 amino acids
-
-
-
additional information
?
-
-
is involved in thalamocortical and corticothalamic signal processing
-
-
-
additional information
?
-
O70196
prolyl oligopeptidase binds to the growth-38 associated protein GAP-43, which is a key regulator of synaptic plasticity
-
-
-
additional information
?
-
-
stimulates the aggregation of alpha-synuclein
-
-
-
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
?
-
Q8VTS9
the specificity for post-proline bonds suggests that the enzyme may play a central role in the hydrolysis of casein-derived bitter peptides, such as beta-casein(f193-209)
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
100% activity at 10 mM
Ca2+
-
Ca2+ shows activating effect on enzyme activity
Ca2+
-
activates
Cu2+
-
-
Fe2+
-
activates
NaBr
-
activates. There are five non-productive binding sites for Cl-, and two for F- and Br-, suggesting that Cl- must bind differently from F- and Br-
NaCl
-
-
NaCl
-
activates. There are five non-productive binding sites for Cl-, and two for F- and Br-, suggesting that Cl- must bind differently from F- and Br-
NaF
-
activates. There are five non-productive binding sites for Cl-, and two for F- and Br-, suggesting that Cl- must bind differently from F- and Br-
Ni2+
-
-
Zinc
the enzyme contains the zinc-dependent metalloprotease motif HEXXH
Zn2+
-
-
Mn2+
-
-
additional information
-
no significant differences between membrane PE and POP regarding the sensitivity to the metals
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
((8'Z)-pentadecenyl)-salicylic acid
-
a noncompetitive inhibitor isolated from Gingko biloba leaves
(+)-gallocatechin
-
IC50: 0.000109 mM, expected to be useful for preventing and curing of Alzheimers disease
(-)-epicatechin
-
IC50: 0.0281 mM, noncompetitive inhibition
(-)-epicatechin 3-O-gallate
-
0.000052 mM, noncompetitive inhibition
(-)-epicatechin gallate
-
IC50: 10.2 mM, expected to be useful for preventing and curing of Alzheimers disease
(-)-epigallocatechin gallate
-
IC50: 0.000142 mM, expected to be useful for preventing and curing of Alzheimers disease
(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
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoic acid
-
93.8% inhibition at 0.5 mM
(2E)-3-(3,4-dimethoxyphenyl)prop-2-enoic acid
-
29.4% inhibition at 0.5 mM
(2E)-3-(4-methoxyphenyl)prop-2-enoic acid
-
less than 10% inhibition at 0.5 mM
(2E)-3-phenylprop-2-enoic acid
-
16.1% inhibition at 0.5 mM
(2E)-3-[3,4-bis(acetyloxy)phenyl]prop-2-enoic acid
-
72.9% inhibition at 0.5 mM
(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-(4-phenylbutanoyl)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidine
-
-
(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)-1-octanoyl-2-(pyrrolidin-1-ylcarbonyl)pyrrolidine
-
-
(2S)-1-[1-(2,3-dihydro-1H-inden-2-ylacetyl)-L-prolyl]pyrrolidine-2-carbaldehyde
-
-
(2S)-1-[1-(2,3-dihydro-1H-inden-2-ylacetyl)-L-prolyl]pyrrolidine-2-carbonitrile
-
-
(2S)-1-[1-(3-[[(2S)-2-(cyclopentylcarbonyl)pyrrolidin-1-yl]carbonyl]benzoyl)-L-prolyl]pyrrolidine-2-carbonitrile
-
-
(2S)-1-[1-(4-phenylbutanoyl)-L-prolyl]pyrrolidine-2-carbaldehyde
-
-
(2S)-1-[1-(4-phenylbutanoyl)-L-prolyl]pyrrolidine-2-carbonitrile
-
-
(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]
-
-
(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
-
-
(3S)-N-benzyl-3-[[(2S)-2-(chloroacetyl)pyrrolidin-1-yl]carbonyl]-3,4-dihydroisoquinoline-2(1H)-carboxamide
-
(4R)-3-octanoyl-4-(pyrrolidin-1-ylcarbonyl)-1,3-thiazolidine
-
-
(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
-
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
(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
(S)-valinyl-(R)-boroproline
-
-
-
1,10-phenanthroline
Lyophyllum cinerascens
-
-
1,10-phenanthroline
-
-
1,2,3,4,6-penta-O-galloyl-beta-D-glucose
-
IC50: 170 nM
1,2,3,4,6-pentagalloyl glucopyranoside
-
specific, noncompetitive, and strong inhibition
1,2,3,6-tetra-O-galloyl-beta-D-glucose
-
IC50: 25 nM
1,2,3,6-tetragalloyl alloside
-
specific, noncompetitive, and strong inhibition
1,2,3-trigalloyl glucopyranoside
-
specific, noncompetitive, and strong inhibition
1,2,6-tri-O-galloylglucose
-
IC50: 0.00044 mM, noncompetitive inhibition
1,2,6-trigalloyl alloside
-
specific, noncompetitive, and strong inhibition
1,2,6-trigalloyl glucopyranoside
-
from Euphorbia helioscopia, specific, noncompetitive, and strong inhibition
1,2-oxazolidin-2-yl[(2S,3aS,7aS)-1-[[(1R,2R)-2-phenylcyclopropyl]carbonyl]octahydro-1H-indol-2-yl]methanone
-
-
1,3,6-trigalloyl alloside
-
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-(2-(1-oxoisoindolin-2-acetyl))-(R)-boroproline
-
-
-
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-(4-phenylbutanoyl)-2(S)-(pyridine-2-carbonyl)pyrrolidine
-
-
1-(4-phenylbutanoyl)-2(S)-(thiophene-2-carbonyl)pyrrolidin
-
-
1-(cyclopent-1-en-1-ylcarbonyl)-N-(2-phenylethyl)-L-prolinamide
-
-
1-(cyclopent-1-enecarbonyl)-D-proline benzylamide
-
-
1-(cyclopent-1-enecarbonyl)-L-proline benzylamide
-
-
1-(cyclopent-1-enecarbonyl)-L-proline phenethylamide
-
-
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
-
-
1-cinnamoylpyrrolidine-2-carboxylic acid
-
14.6% inhibition at 0.5 mM
-
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
-
-
1-[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]-2-[(2R)-1,2,3,4-tetrahydronaphthalen-2-yl]ethanone
-
-
1-[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]-2-[(2S)-1,2,3,4-tetrahydronaphthalen-2-yl]ethanone
-
-
1-[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]-4-(thiophen-2-yl)butan-1-one
-
-
1-[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]octan-1-one
-
-
1-[2-oxo-2-[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]ethyl]-3-phenylquinoxalin-2(1H)-one
-
-
1-[[(2S)-1-(4-phenylbutanoyl)pyrrolidin-2-yl]carbonyl]pyrrolidin-2-one
-
-
2',4'-dihydroxy-6'-methoxy-3',5'-dimethylchalcone
-
50% inhibition at 0.15 mM
2',4'-dihydroxy-6'-methoxy-3',5'-dimethyldihydrochalcone
-
50% inhibition at 0.098 mM
2',4'-dihydroxy-6'-methoxy-3'-methylchalcone
-
50% inhibition at 0.0375 mM
2',4'-dihydroxy-6'-methoxy-3'-methyldihydrochalcone
-
50% inhibition at 0.0125 mM
2'-hydroxy-4',6'-dimethoxy-3'-methylchalcone
-
50% inhibition above 0.2 mM
2'-hydroxy-4',6'-dimethoxy-3'-methyldihydrochalcone
-
50% inhibition at 0.158 mM
2(S)-(aroyl)-1-(4-phenylbutanoyl)pyrrolidines
-
-
-
2(S)-(cycloalk-1-enecarbonyl)-1-(4-phenyl-butanoyl)pyrrolidines
-
-
-
2(S)-(cyclohex-1-enecarbonyl)-1-(4-phenylbutanoyl)pyrrolidine
-
-
2(S)-(cyclopent-1-enecarbonyl)-1-(4-phenylbutanoyl)pyrrolidine
-
-
2(S)-(furan-2-carbonyl)-1-(4-phenylbutanoyl)pyrrolidine
-
-
2,3-dihydro-1H-inden-2-yl[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]methanone
-
-
2,3-dihydro-1H-pyrrol-1-yl[(2S,3aS,7aS)-1-[[(1R,2R)-2-phenylcyclopropyl]carbonyl]octahydro-1H-indol-2-yl]methanone
-
-
2,5-dihydro-1H-pyrrol-1-yl[(2S,3aS,7aS)-1-[[(1R,2R)-2-phenylcyclopropyl]carbonyl]octahydro-1H-indol-2-yl]methanone
-
-
2-(2,3-dihydro-1H-inden-2-yl)-1-[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]ethanone
-
-
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-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
2-mercaptoethanol
-
-
2-oxo-kolavenic acid
-
terpenoid from the bark of Xylopia aethiopia, 34% inhibition at 1mM
2-[2-oxo-2-[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]ethyl]-1H-isoindole-1,3(2H)-dione
-
-
2-[2-[(2S)-4,4-difluoro-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]-2-oxoethyl]-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-dimethyl glutaric acid bis(L-prolyl-pyrrolidine) amide
-
IC50: 13 nM
3,4-dichloroisocoumarin
-
enzyme from lymphocyte
3,5,4'-trihydroxystilbene 4'-O-beta-D-(2-O-galloyl)glucopyranoside
-
IC50: 0.003 mM, noncompetitive inhibition
3,5,4'-trihydroxystilbene 4'-O-beta-D-(6-O-galloyl)glucopyranoside
-
IC50: 0.0149 mM, noncompetitive inhibition
3,5,4'-trihydroxystilbene 4'-O-beta-D-glucopyranoside
-
IC50: 0.0229 mM, noncompetitive inhibition
3-(2(S)-benzoyl-pyrrolidine-1-carbonyl)-benzoyl-5(R)-tert-butyl-L-Pro-pyrrolidine
-
IC50: 460 nM
3-(2(S)-benzoyl-pyrrolidine-1-carbonyl)-benzoyl-L-Pro-pyrrolidine
-
IC50: 18 nM
3-(2,3-dihydro-1H-inden-2-yl)-1-[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]propan-1-one
-
-
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-({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
-
-
3-cyclohexyl-N-[(2S)-1-oxo-3-phenyl-1-[(2S)-2-(piperidin-1-ylcarbonyl)pyrrolidin-1-yl]propan-2-yl]propanamide
-
-
3-O-galloylepigallocatechin-(4-8)-epigallocetechin 3-O-gallate
-
IC50: 440 nM
3-[3-oxo-3-[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]propyl]-5,5-diphenylimidazolidine-2,4-dione
-
-
33mer of gluten-derived peptide
-
-
4-(2,3-dihydro-1H-inden-2-yl)-1-[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]butan-1-one
-
-
4-(2-aminoethyl)-benzenesulfonyl fluoride
-
-
4-(2-aminoethyl)benzenesulfonyl fluoride
-
inhibition of extracellular isozyme
4-(4-chlorophenyl)-8-(ethoxycarbonyl)-5-methyl-2,3-dihydrofuro[3,2-c]quinolin-5-ium iodide
-
-
4-(4-hydroxyphenyl)-2-butanone 4'-O-beta-D-(2,6-di-O-galloyl)glucopyranoside
-
IC50: 0.0105 mM, noncompetitive inhibition
4-(4-hydroxyphenyl)-2-butanone 4'-O-beta-D-(2-O-galloyl-6-O-cinnamoyl)glucopyranoside
-
IC50: 690 nM, noncompetitive inhibition
4-(4-hydroxyphenyl)-2-butanone 4'-O-beta-D-(6-O-galloyl-2-O-cinnamoyl)glucopyranoside
-
IC50: 0.082 mM, noncompetitive inhibition
4-(4-iodophenyl)butanoyl-L-prolyl-pyrrolidine
-
-
-
4-(4-[123I]iodophenyl)butanoyl-L-prolyl-2(S)-cyanopyrrolidine
-
-
-
4-([[(3S)-8-acetyl-5-oxo-3-(pyrrolidin-1-ylcarbonyl)-1,2,3,5-tetrahydroindolizin-6-yl]oxy]methyl)benzonitrile
-
-
4-chloromercuribenzoaic acid
-
14% residual activity at 0.2 mM
-
4-Chloromercuriphenylsulfonate
-
-
4-Chloromercuriphenylsulfonate
-
weak
4-Chloromercuriphenylsulfonate
-
not
4-Chloromercuriphenylsulfonate
-
-
4-Chloromercuriphenylsulfonate
-
-
4-hydroxymercuriphenylsulfonate
-
-
4-phenyl-1-[(2S)-2-(pyrrolidin-1-ylmethyl)pyrrolidin-1-yl]butan-1-one
-
-
4-phenyl-1-[(2S)-2-[[(2S)-2-(1,3-thiazol-2-ylcarbonyl)pyrrolidin-1-yl]carbonyl]pyrrolidin-1-yl]butan-1-one
-
-
4-phenyl-1-[(3S)-3-(pyrrolidin-1-ylcarbonyl)-3,4-dihydroisoquinolin-2(1H)-yl]butan-1-one
-
-
4-phenyl-1-[(4R)-4-(1,3-thiazolidin-3-ylcarbonyl)-1,3-thiazolidin-3-yl]butan-1-one
-
-
4-phenyl-1-[(4S)-4-(1,3-thiazolidin-3-ylcarbonyl)-1,3-thiazolidin-3-yl]butan-1-one
-
-
4-phenyl-1-[2-(pyrrolidin-1-ylcarbonyl)cyclopent-1-en-1-yl]butan-1-one
-
-
4-phenyl-1-[5-(pyrrolidin-1-ylcarbonyl)cyclopent-1-en-1-yl]butan-1-one
-
-
4-phenyl-butanoyl-L-prolyl-2(S)-cyanopyrrolidine
-
KYP-2047
4-phenyl-butanoyl-L-prolyl-2(S)-cyanopyrrolidine
-
KYP-204, 0.1 mM and 0.5 mM concentrations significantly inhibit enzyme activity in tissue homogenate
4-phenylbutanoyl-2(S)-(2-oxocyclopentanecarbonyl)-pyrrolidine
-
IC50: 260 nM
4-phenylbutanoyl-2(S)-(3-phenylpropionyl)pyrrolidine
-
IC50: 0.024 mM
4-phenylbutanoyl-2(S)-(cyclohexanecarbonyl)pyrrolidine
-
IC50: 1100 nM
4-phenylbutanoyl-2(S)-(cyclopentanecarbonyl)pyrrolidine
-
IC50: 30 nM
4-phenylbutanoyl-2(S)-(phenylacetyl)pyrrolidine
-
IC50: 3600 nM
4-phenylbutanoyl-2(S)-benzylpyrrolidine
-
IC50: 23 nM
4-phenylbutanoyl-2(S)-isobutanoylpyrrolidine
-
IC50: 620 nM
4-phenylbutanoyl-5(R)-methyl-L-Pro-2(S)-(hydroxyacetyl)pyrrolidine
-
IC50: 0.15 nM
4-phenylbutanoyl-5(R)-methyl-L-Pro-pyrrolidine
-
IC50: 0.71 nM
4-phenylbutanoyl-5(R)-t-butyl-L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine
-
-
4-phenylbutanoyl-5(R)-t-butyl-L-prolyl-pyrrolidine
-
-
4-phenylbutanoyl-5(R)-tert-butyl-L-Pro-2(S)-(hydroxyacetyl)-pyrrolidine
-
IC50: 0.26 nM
4-phenylbutanoyl-5(R)-tert-butyl-L-Pro-pyrrolidine
-
IC50: 1.2 nM
4-phenylbutanoyl-5(R)-tert-butyl-L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine
-
-
-
4-phenylbutanoyl-5(S)-methyl-L-Pro-pyrrolidine
-
IC50: 1.4 nM
4-phenylbutanoyl-L-Pro-2(S)-(hydroxyacetyl)-pyrrolidine
-
IC50: 0.24 nM
4-phenylbutanoyl-L-Pro-pyrrolidine
-
IC50: 2.2 nM
4-phenylbutanoyl-L-prolyl-2(S)-(cyclopentanecarbonyl)-pyrrolidine
-
IC%0: 1010 nM
4-phenylbutanoyl-L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine
-
IC50: 0.2 nM
4-phenylbutanoyl-L-prolyl-2(S)-acetylpyrrolidine
-
IC50: 170 nM
4-phenylbutanoyl-L-prolyl-2(S)-benzoylpyrrolidine
-
IC50: 210 nM
4-phenylbutanoyl-L-prolyl-2(S)-cyanopyrrolidine
-
-
-
4-phenylbutanoyl-L-prolyl-2(S)cyanopyrrolidine
-
-
4-phenylbutanoyl-L-prolyl-pyrrolidine
-
i.e. SUAM-1221
4-toluenesulfonamide
-
98% residual activity at 0.2 mM
5,5'-dithio-bis(2-nitrobenzoic acid)
-
enzyme from brain
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
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
6-(10Z-heptadecenyl)salicylic acid
-
isolated from leaves of Ginkgo biloba, noncompetitive, 50% inhibition at 0.00062 mM
6-(8Z-pentadecenyl)salicylic acid
-
isolated from leaves of Ginkgo biloba, noncompetitive, 50% inhibition at 0.00086 mM
7-hydroxy-5-methoxy-6,8-dimethylflavanone
-
14% inhibition at 0.5 mM
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
-
-
9H-fluoren-9-ylmethyl [(2S)-5-carbamimidamido-1-[(2S)-2-cyanopyrrolidin-1-yl]-1-oxopentan-2-yl]carbamate
-
-
acetonyl geraniin
-
specific, noncompetitive, and strong inhibition
acetyl-5(R)-tert-butyl-L-Pro-pyrrolidine
-
IC50: 7100 nM
adipic acid bis(L-prolyl-pyrrolidine) amide
-
IC50: 68 nM
AEBSF
1 mM, 12% inhibition
aesculitannin B
-
noncompetitive
Al3+
-
65% residual activity at 10 mM
Al3+
-
34.5% residual activity at 1 mM
Al3+
-
-
alpha-/beta-carotene
-
mixture of alpha- and beta-form, 64.4% inhibition at 0.5 mM
alpha-ketobenzothiazol
-
enzyme from serum
alpha1-casein
-
-
-
alpha2-gliadin 33-mer peptide
-
POP inhibitor
-
amastatin
-
0.1 mM, 97% inhibition
Aprotinin
-
inhibition of extracellular isozyme
Aprotinin
-
89% residual activity at 1 mM
arachidonic acid
-
50% inhibition at 0.0534 mM
ARI-3099
-
i.e. N-(pyridine-4-carbonyl)-D-Ala-boro-L-Pro
-
ARI-3531
-
selective inhibitor, i.e. N-(pyridine-3-carbonyl)-L-Val-boroproline
-
bacitracin
-
-
bacitracin
-
50% inhibition at 0.129 mM
bacitracin
-
50% inhibition at 0.130 mM
bacitracin
-
-
Baicalin
-
-
benzamidine
1 mM, 7.2% inhibition
benzoyl-L-Pro-pyrrolidine
-
IC50: 66 nM
benzyl (1S,2S)-2-[[(2S)-2-formylpyrrolidin-1-yl]carbonyl]cyclohexanecarboxylate
-
-
benzyl (2S)-2-(1,3-oxazolidin-3-ylcarbonyl)pyrrolidine-1-carboxylate
-
-
benzyl (2S)-2-(1,3-thiazolidin-3-ylcarbonyl)pyrrolidine-1-carboxylate
-
-
benzyl (2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidine-1-carboxylate
-
-
benzyl (2S)-2-([(2S)-2-[(5-phenyl-4,5-dihydro-1,2-oxazol-3-yl)carbonyl]pyrrolidin-1-yl]carbonyl)pyrrolidine-1-carboxylate
-
benzyl (2S)-2-[(1-oxido-1,3-thiazolidin-3-yl)carbonyl]pyrrolidine-1-carboxylate
-
-
benzyl (2S)-2-[[(2S)-2-(hydroxymethyl)pyrrolidin-1-yl]carbonyl]pyrrolidine-1-carboxylate
-
-
benzyl (2S)-2-[[(2S)-2-([5-[(benzyloxy)methyl]-1,2-oxazol-3-yl]carbonyl)pyrrolidin-1-yl]carbonyl]pyrrolidine-1-carboxylate
-
benzyl (2S)-2-[[(2S)-2-([5-[(benzyloxy)methyl]-4,5-dihydro-1,2-oxazol-3-yl]carbonyl)pyrrolidin-1-yl]carbonyl]pyrrolidine-1-carboxylate
-
benzyl (2S)-2-[[(2S)-2-formylpyrrolidin-1-yl]carbonyl]-2,3-dihydro-1H-indole-1-carboxylate
-
-
benzyl (2S)-2-[[(2S)-2-formylpyrrolidin-1-yl]carbonyl]-5-oxopyrrolidine-1-carboxylate
-
-
benzyl (2S)-2-[[(2S)-2-formylpyrrolidin-1-yl]carbonyl]pyrrolidine-1-carboxylate
-
-
benzyl trachyloban-19-oic acid
-
terpenoid from the bark of Xylopia aethiopia, 50% inhibition at 0.037 mM
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,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
benzyl [(3R,6R,7aS)-3-cyano-5-oxohexahydropyrrolo[2,1-b][1,3]thiazol-6-yl]carbamate
-
-
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-(chloroacetyl)pyrrolidin-1-yl]-2-oxoethyl]carbamate
-
-
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
benzylcarbamoyl-5(R)-tert-butyl-L-prolyl-pyrrolidine
-
IC50: 2.0 nM
benzylcarbamoyl-L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine
-
-
-
Benzyloxycarbonyl-Ala-Ala-Pro diazomethyl ketone
-
-
benzyloxycarbonyl-Gly-Gly-Pro-CH2Cl
-
enzyme from kidney
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide
-
-
benzyloxycarbonyl-Gly-Pro-CH2Cl
-
-
benzyloxycarbonyl-Gly-Pro-CH2Cl
Agaricus bisporus, Ascidia sp., Bos taurus, Lyophyllum cinerascens
-
-
benzyloxycarbonyl-Gly-Pro-CH2Cl
-
enzyme from kidney and brain
benzyloxycarbonyl-L-methionyl-2(S)-cyanopyrrolidine
-
-
benzyloxycarbonyl-L-Pro-L-prolinal
-
IC50: 0.4 nM
benzyloxycarbonyl-Pro-L-prolinal
-
IC50: 0.33 nM
benzyloxycarbonyl-Pro-Pro-OH
-
-
benzyloxycarbonyl-Pro-prolinal
Lyophyllum cinerascens
-
-
benzyloxycarbonyl-Pro-prolinal
-
i.e. Z-Pro-prolinal
benzyloxycarbonyl-Pro-prolinal
-
i.e. Z-Pro-Prolinal, inhibition of cytsolic isozyme, but no inhibition of the extracellular isozyme in serum
benzyloxycarbonyl-Pro-prolinal
-
i.e. Z-Pro-prolinal
benzyloxycarbonyl-Pro-prolinal
-
-
benzyloxycarbonyl-Pro-prolinal
-
benzyloxycarbonyl-Pro-prolinal
-
-
benzyloxycarbonyl-Pro-prolinal
-
-
benzyloxycarbonyl-Pro-prolinal
-
-
benzyloxycarbonyl-Pro-prolinal
-
-
benzyloxycarbonyl-Pro-pyrrolidine
-
-
benzyloxycarbonyl-Pro-thiazolidine
-
-
benzyloxycarbonyl-proline-prolinal
-
specific inhibition
benzyloxycarbonyl-thioPro-thiazoidine
-
-
-
benzyloxycarbonyl-thioPro-thioprolinal
-
-
-
benzyloxycarbonyl-thioprolyl-thioprolinal
-
specific inhibitor of prolyl oligopeptidase
benzyloxycarbonyl-thioprolylthiazolidine
-
-
benzyloxycarbonyl-thioprolylthioprolinal
-
enzyme from lymphocyte
Berberine
-
-
bestatin
-
0.5 mM, 97% inhibition
betulin
-
50% inhibition at 0.101 mM
bixanin
-
specific and noncompetitive inhibition
Boc-5(R)-tert-butyl-L-Pro-pyrrolidine
-
IC50: 2.2 nM
Boc-5(S)-tert-butyl-L-Pro-pyrrolidine
-
IC50: 9.2 nM
Boc-Asn-Phe-Pro-aldehyde
-
-
Boc-Asn-Phe-Pro-aldehyde
-
-
Boc-L-Pro-pyrrolidine
-
IC50: 29 nM
buspirone
-
25% inhibition at 0.01 mM
Ca2+
-
-
Ca2+
-
-
calcitonin gene-related peptide
-
-
-
caproyl-L-Pro-((2S)-hydroxyacetyl)pyrrolidine
-
-
carbamazepine
-
mechanism, reverses the effect of drugs
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
Cd2+
-
enzyme from lymphocyte
Chloromethylketone derivatives
-
-
Chloromethylketone derivatives
-
-
Chloromethylketone derivatives
-
-
Chloromethylketone derivatives
-
-
chlorpromazine
-
55% inhibition at 0.01 mM
cis-3,5,4'-trihydroxystilbene 4'-O-beta-D-(6-O-galloyl)glucopyranoside
-
IC50: 0.0028 mM, noncompetitive inhibition
citalopram
-
27% inhibition at 0.01 mM
clozapine
-
40% inhibition at 0.01 mM
Co2+
-
-
Co2+
-
enzyme from lymphocyte
Co2+
-
48% residual activity at 0.2 mM
Co2+
-
-
corilagin
-
specific, noncompetitive, and strong inhibition
Cu2+
-
enzyme from lymphocyte
Cu2+
-
enzyme from brain
Cu2+
-
enzyme from skin
Cu2+
-
12% residual activity at 1 mM
Cu2+
-
14.1% residual activity at 1 mM
Cu2+
-
13% residual activity at 0.2 mM
Cu2+
-
-
Cu2+
-
-
Cu2+
-
-
Cu2+
-
-
cyclopent-2-ene-1,2-dicarboxylic acid 2-benzylamide 1-[2(S)-(hydroxyacetyl)-H-pyrrolidine]amide
-
-
-
cyclosporine A
-
the activating effect of methotrexate dominates the inhibitory effect of cyclosporine A
desipramine
-
20% inhibition at 0.01 mM
DFP
0.1 mM, 100% inhibition
diethyl dicarbonate
-
enzyme from brain
diethyldicarbonate
-
-
diisopropyl fluorophosphate
Agaricus bisporus, Ascidia sp.
-
-
diisopropyl fluorophosphate
-
enzyme from hypophysis, eye-lens and brain
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
enzyme from brain, lymphocyte and serum
diisopropyl fluorophosphate
Lyophyllum cinerascens, Mus musculus, Novosphingobium capsulatum
-
-
diisopropyl fluorophosphate
-
enzyme from kidney and brain
diisopropyl fluorophosphate
-
enzyme from brain and skin
diisopropyl fluorophosphate
-
enzyme from brain and muscle
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
13% residual activity at 0.2 mM
diisopropylfluorophosphate
-
-
diisopropylfluorophosphate
-
-
diisopropylfluorophosphate
-
-
diisopropylfluorophosphate
-
-
diisopropylfluorophosphate
-
-
diisopropylfluorophosphate
-
-
diisopropylfluorophosphate
-
-
diisopropylfluorophosphate
-
-
diisopropylfluorophosphate
-
-
diisopropylfluorophosphate
-
-
diisopropylfluorophosphate
-
-
diisopropylfluorophosphate
-
-
diprotin
-
0.1 mM, complete inhibition
Diprotin A
-
-
dithiothreitol
-
-
docosahexaenoic acid
-
50% inhibition at 0.0462 mM
duloxetine
-
21% inhibition at 0.01 mM
E-64
Lyophyllum cinerascens
-
-
EDTA
-
-
EDTA
Lyophyllum cinerascens
-
-
EDTA
-
37.3% residual activity at 10 mM
EDTA
-
93% residual activity at 0.2 mM
eicosapentaenoic acid
-
50% inhibition at 0.0994 mM
elaeocarpusin
-
specific, noncompetitive, and strong inhibition
Elastatinal
-
partially
ent-kaur-16-en-19-oic acid
-
terpenoid from the bark of Xylopia aethiopia, 50% inhibition at 0.060 mM
epi-betulinic acid
-
50% inhibition at 0.015 mM
escitalopram
-
39% inhibition at 0.01 mM
euphorscopin
-
specific, noncompetitive, and strong inhibition
Fe2+
-
55% residual activity at 10 mM
Fe2+
-
80.6% residual activity at 1 mM
fluoxetine
-
an antidepressant
flupenthixol
-
56% inhibition at 0.01 mM
gallic acid 4-O-beta-D-(6-O-galloyl)glucopyranoside
-
IC50: 0.00939 mM, noncompetitive inhibition
geraniin
-
specific, noncompetitive, and strong inhibition
ginkgolic acid
-
-
glutaric acid bis(L-prolyl-pyrrolidine) amide
-
IC50: 48 nM
glycinyl-(R)-boroproline
-
-
-
Heavy metal ions
-
-
-
helioscopin B
-
specific, noncompetitive, and strong inhibition
helioscopinin A
-
specific, noncompetitive, and strong inhibition
helioscopinin B
-
specific, noncompetitive, and strong inhibition
hetero-chitooligosaccharides
-
hetero-chitooligosaccharides with different degrees of sulfatization, or deacetylation, preparation and inhibitory potency, competitive enzyme inhibition, overview
-
Hg2+
-
enzyme from hypophysis and brain
Hg2+
-
enzyme from lymphocyte
Hg2+
Lyophyllum cinerascens
-
-
Hg2+
-
enzyme from brain
Hg2+
-
complete inhibition at 0.2 mM
Hg2+
-
-
Hg2+
-
-
Hg2+
-
-
hispidulin
-
0.1 mM, 43% enzyme inhibition
imipramine
-
29% inhibition at 0.01 mM
interferon-alpha
-
IFN-alpha
-
iodoacetamide
-
enzyme from brain
iodoacetamide
-
enzyme from kidney
iodoacetamide
-
enzyme from brain
iodoacetamide
-
87% residual activity at 0.2 mM
iodoacetamide
-
-
iodoacetate
Lyophyllum cinerascens
-
-
iodoacetate
-
enzyme from brain
iodoacetate
-
weak
isolinderalactone
-
competitive
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)-acetylpyrrolidine L-prolyl-pyrrolidine amide
-
IC50: 65 nM
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)-benzoylpyrrolidine L-prolyl-pyrrolidine amide
-
IC50: 18 nM
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(L-prolyl-pyrrolidine) amide
-
IC50: 26 nM
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 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 bis-2(S)-acetylpyrrolidine amide
-
54% inhibition at 0.1 nM
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
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
isophthalic acid L-prolylbenzylamine L-prolyl-pyrrolidine amide
-
IC50: 31 nM
jolkinin
-
specific, noncompetitive, and strong inhibition
JTP-4819
-
IC50: 0.2 nM
JTP-4819
-
i.e. (S)-2-[[(S)-2-(hydroxyacetyl)-1-yrrolidinyl]carbonyl]-N-(phenylmethyl)-1-pyrrolidinecarboxamide
JTP-4819
-
i.e. (S)-2-[[(S)-2-(hydroxyacetyl)-1-yrrolidinyl]carbonyl]-N-(phenylmethyl)-1-pyrrolidinecarboxamide, improves learning deficits in rats with dorsal hippocampal lesions
JTP-4819
-
a selective POP inhibitor, physiological effects, overview
JTP-4819
-
-
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
K+
-
92.2% residual activity at 1 mM
ketanserin
-
mixed type inhibitor, 49% inhibition at 0.01 mM
kinapsin-24
-
-
kolavenic acid
-
terpenoid from the bark of Xylopia aethiopia, 50% inhibition at 0.099 mM
KYP-2047
-
i.e. 4-phenylbutanoyl-L-prolyl-2(S)cyanopyrrolidine
KYP-2047
-
i.e. 4-phenylbutanoyl-l-prolyl-2(S)-cyanopyrrolidine, highly potent covalent reversible competitive inhibitor
KYP-2047
-
i.e. 4-phenylbutanoyl-L-prolyl-(2S)-cyanopyrrolidine
KYP-2047
-
i.e. 4-phenylbutanoyl-l-prolyl-2(S)-cyanopyrrolidine
KYP-2047
-
-
L-1-tosylamido-2-phenylethylchloromethyl ketone
-
-
lamotrigine
-
22% inhibition at 0.01 mM
Leupeptin
0.1 mM, 46.2% inhibition
leupeptin hemisulfate
-
86% residual activity at 1 mM
-
levomepromazine
-
32% inhibition at 0.01 mM
licuroside
-
IC50: 0.0265 mM, noncompetitive inhibition
linderene acetate
-
competitive
linoleic acid
-
50% inhibition at 0.0438 mM
lithium
-
reverses the effect of the drugs
lithium
-
mechanism, reverses the effect of drugs
lupeol
-
50% inhibition at 0.065 mM
lupeol
-
0.1 mM, 5% enzyme inhibition
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 (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate
-
90.5% inhibition at 0.5 mM
methyl (2E)-3-(4-methoxyphenyl)prop-2-enoate
-
22% inhibition at 0.5 mM
methyl (2E)-3-phenylprop-2-enoate
-
20% 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
-
-
methyl trachyloban-19-oic acid
-
terpenoid from the bark of Xylopia aethiopia, 50% inhibition at 0.045 mM
Mg2+
-
97% residual activity at 10 mM
Mg2+
-
87.3% residual activity at 1 mM
mianserin
-
15% inhibition at 0.01 mM
Mn2+
-
30% residual activity at 10 mM
Mn2+
-
24.3% residual activity at 1 mM
N-(1-naphthalenecarbonyl)glycinyl-(R)-boroproline
-
-
-
N-(benzoyl)-(R)-alaninyl-(R)-boroproline
-
-
-
N-(pyridine-2-chloro-4-carbonyl)-(R)-alaninyl-(R)-boroproline
-
-
-
N-(pyridine-2-fluoro-4-carbonyl)-(R)-alaninyl-(R)-boroproline
-
-
-
N-(pyridine-3-carbonyl)-(R)-alaninyl-(R)-boroproline
-
-
-
N-(pyridine-3-carbonyl)glycinyl-(R)-boroproline
-
-
-
N-(pyridine-3-chloro-4-carbonyl)-(R)-alaninyl-(R)-boroproline
-
-
-
N-(pyridine-3-fluoro-4-carbonyl)-(R)-alaninyl-(R)-boroproline
-
-
-
N-(pyridine-4-carbonyl)glycinyl-(R)-boroproline
-
-
-
N-(quinoline-4-carbonyl)-(R)-alaninyl-(R)-boroproline
-
-
-
N-(quinoline-4-carbonyl)-(R)-butyl(glycinyl)-(R)-boroproline
-
-
-
N-(quinoline-4-carbonyl)-(R)-ethyl(glycinyl)-(R)-boroproline
-
-
-
N-(quinoline-4-carbonyl)-(R)-methioninyl-(R)-boroproline
-
-
-
N-(quinoline-4-carbonyl)-(R)-phenyl(glycinyl)-(R)-boroproline
-
-
-
N-(quinoline-4-carbonyl)-(R)-propyl(glycinyl)-(R)-boroproline
-
-
-
N-(quinoline-4-carbonyl)-(R)-serinyl-(R)-boroproline
-
-
-
N-acetyl-(R)-alaninyl-(R)-boroproline
-
-
-
N-Alpha-benzyloxycarbonyl-Ala-Pro
-
-
N-benzyloxycarbonyl-L-prolyl-L-prolinal
-
i.e. Z-Pro-prolinal
N-benzyloxycarbonyl-thioprolyl-thioprolinaldimethylacetal
-
-
-
N-Benzyloxycarbonyl-valyl-prolinal
-
-
N-carbobenzoxy-Leu-Leu-Leu-COH
-
the proteasome inhibitor
N-carbobenzoxy-prolyl-prolinal
-
ZPP
N-ethylmaleimide
-
50% residual activity at 0.2 mM
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
N-[(2S)-1-[(2S)-2-formylpyrrolidin-1-yl]-3-methyl-1-oxobutan-2-yl]-4-phenylbutanamide
-
-
N-[(2S)-3-methyl-1-oxo-1-[(2S)-2-(piperidin-1-ylcarbonyl)pyrrolidin-1-yl]butan-2-yl]-3-phenoxybenzamide
-
-
Na+
-
93.1% residual activity at 1 mM
NEM
-
enzyme from hypophysis and eye-lens
NEM
-
enzyme from brain and skin
Ni2+
-
86% residual activity at 0.2 mM
Ni2+
-
-
o-phenanthroline
-
-
o-phenanthroline
-
79% residual activity at 0.2 mM
oleic acid
-
50% inhibition at 0.0236 mM
oleic acid
-
50% inhibition at 0.031 mM
ONO-1603
-
-
ONO-1603
-
-
orinithine decarboxylase
-
-
-
oroxylin A
-
0.1 mM, 20% enzyme inhibition
oroxyloside
-
0.1 mM, 34% enzyme inhibition
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
Pancreatic basic trypsin inhibitor
-
-
-
PCMB
-
-
PCMB
-
enzyme from brain
PCMB
-
enzyme from lymphocyte
PCMB
Lyophyllum cinerascens
-
-
PCMB
-
enzyme from kidney and brain
PCMB
-
enzyme from brain and skin
PCMB
-
enzyme from brain
PCMB
0.1 mM, 98% inhibition
PCMBS
-
enzyme from kidney
phenyl (2S)-2-(((2S)-2-(1,3-thiazol-2-ylcarbonyl)pyrrolidin-1-yl)carbonyl)pyrrolidine-1-carboxylate
-
phenyl (2S)-2-(((2S)-2-(isoxazol-3-ylcarbonyl)pyrrolidin-yl)carbonyl)pyrrolidine-1-carboxylate
-
phenyl (2S)-2-([(2S)-2-[(5-phenylisoxazol-3-yl)carbonyl]pyrrolidin-1-yl]carbonyl)pyrrolidine-1-carboxylate
-
phenyl (2S)-2-[[(2S)-2-([5-[(2E)-3-phenylprop-2-en-1-yl]isoxazol-3-yl]carbonyl)pyrrolidin-1-yl]carbonyl]pyrrolidine-1-carboxylate
50% inhibition at 0.01 mM, inhibition of parasite invasion into host cells
phenyl (2S)-2-[[(2S)-2-[[5-(trimethylsilyl)isoxazol-3-yl]carbonyl]pyrrolidin-1-yl]carbonyl]pyrrolidine-1-carboxylate
-
phenylmethanesulfonyl fluoride
-
PE and POP are partially resistant to phenylmethanesulfonyl fluoride, a generic serine protease inhibitor that has a low efficiency in inhibiting POP
phenylmethylsulfonyl fluoride
-
-
phenylmethylsulfonyl fluoride
-
97% residual activity at 1 mM
phenylmethylsulfonyl fluoride
-
-
phenylmethylsulfonyl fluoride
-
-
phenylmethylsulfonyl fluoride
-
-
phthalic acid bis(L-prolyl-pyrrolidine) amide
-
IC50: 0.021 mM
pimozide
-
11% inhibition at 0.01 mM
PMSF
Ascidia sp.
-
-
PMSF
-
enzyme from lymphocyte
PMSF
Lyophyllum cinerascens
-
-
PMSF
-
enzyme from brain and partly enzyme from skin
PMSF
1 mM, 18% inhibition
prazosin
-
91% inhibition at 0.01 mM
prochlorperazine
-
77% inhibition at 0.01 mM
promazine
-
64% inhibition at 0.01 mM
propeptin
-
a netural inhibitor of POP isolated from Microbispora sp. strain SNA-115
puromycin
-
0.1 mM, 97% inhibition
reboxetine
-
13% inhibition at 0.01 mM
reserpine
-
18% inhibition at 0.01 mM
rhodionin
-
IC50: 0.022 mM
rhodiosin
-
IC50: 0.041 mM
risperidone
-
56% inhibition at 0.01 mM
ritanserin
-
33% inhibition at 0.01 mM
rosiridin
-
IC50: 840 nM
rosmarinic acid
-
non-competitive inhibitor
rugosin E
-
from Euphorbia supina, specific, noncompetitive, and strong inhibition
S 17092
-
selective enzyme inhibitor, pharmacodynamics and pharmacokinetics, overview
S 17092
-
physiological effects, overview
S-17092
-
i.e. (2S,3aS,7aS)-1-[[(R,R)-2-phenylcyclopropyl]carbonyl]-2-[(thiazolidin-3-yl)carbonyl] octahydro-1H-indole
S-17092
-
i.e. (2S,3aS,7aS)-1-[(R,R)-2-phenylcyclopropyl]-2-[(thiazolidin-3-yl)carbonyl]octahydro-1H-indole, specific enzyme inhibitor
S17092
-
-
salicylic acid
-
50% inhibition at 1.65 mM
Sn2+
-
87% residual activity at 0.2 mM
staurosporine
-
-
SUAM-1221
-
IC50: 2 nM
SUAM-1221
-
IC50: 2.2 nM
SUAM-14746
-
-
-
succinic acid bis(L-prolyl-pyrrolidine) amide
-
IC50: 77 nM
supinanin
-
specific, noncompetitive, and strong inhibition
teracatain
-
specific, noncompetitive, and strong inhibition
terephthalic acid bis(L-prolyl-pyrrolidine) amide
-
IC50: 81 nM
tert-butyl (2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidine-1-carboxylate
-
-
tert-butyl [(2S)-3-methyl-1-(1,3-thiazolidin-3-yl)-1-thioxobutan-2-yl]carbamate
-
-
thioridazine
-
non-competitive inhibitor, 91% inhibition at 0.01 mM
TLCK
0.1 mM, 73.2% inhibition
tosyllysylchloromethane
-
enzyme from brain
tosylphenylalanylchloromethane
-
enzyme from brain, partly
TPCK
0.1 mM, 91.1% inhibition
trachyloban-19-oic acid
-
terpenoid from the bark of Xylopia aethiopia, 50% inhibition at 0.164 mM
Tyr-Pro-Ile-Pro-Phe
-
inhibitory peptide isolated from grapes of Cabernet Sauvignon
UAMC-00021
-
-
Val-Glu-Ile-Pro-Glu
-
inhibitory peptide isolated from grapes of Cabernet Sauvignon
Valproate
-
competitive inhibitor, 56% inhibition at 0.5 mM
Valproic acid
-
an antimanic drug
Valproic acid
-
reverses the effect of the drugs
Valproic acid
-
mechanism, reverses the effect of drugs
verbascoside
-
-
Z-Ala-Pro
-
-
Z-L-Pro-prolinal
-
50% inhibition at 0.0000022 mM
Z-L-prolyl-L-prolinal
-
-
Z-Pro-Pro-aldehyde-dimethyl acetal
-
Z-Pro-Pro-aldehyde-dimethylacetal
-
-
Z-Pro-Pro-dimethyl acetal aldehyde
-
irreversible inhibitor
Z-Pro-prolinal
-
a transition state analog inhibitor, binding structure
Z-Pro-prolinal
-
-
Z-Pro-prolinal
-
physiological effects, overview
Z-Pro-prolinal
-
with high potency but relatively poor stability
Z-Pro-prolinal
-
-
Z-Pro-prolinal
-
-
Z-proline prolinal
-
-
Z-prolyl-prolinal
-
-
-
Z-proyl-prolinal
-
-
-
Z-thioprolyl-thioprolinal-dimethylacetal
-
physiological effects, overview
Zn2+
-
partly
Zn2+
-
enzyme from lymphocyte
Zn2+
-
enzyme from skin
Zn2+
-
91% residual activity at 10 mM
Zn2+
-
31.2% residual activity at 1 mM
Zn2+
-
61% residual activity at 0.2 mM
Zn2+
-
-
Zn2+
-
-
Zn2+
-
-
ZTTA
-
i.e. N-benzyloxycarbonyl-thioprolyl-thioprolinal-dimethylacetal
[(1R,2R)-2-phenylcyclopropyl][(2S,3aS,7aS)-2-(1,3-thiazolidin-3-ylcarbonyl)octahydro-1H-indol-1-yl]methanone
-
-
[(1R,2R)-2-phenylcyclopropyl][(2S,3aS,7aS)-2-(1H-pyrrol-1-ylcarbonyl)octahydro-1H-indol-1-yl]methanone
-
-
[(1R,2R)-2-phenylcyclopropyl][(2S,3aS,7aS)-2-(pyrrolidin-1-ylcarbonyl)octahydro-1H-indol-1-yl]methanone
-
-
[(1R,2R)-2-phenylcyclopropyl][(3S)-3-(pyrrolidin-1-ylcarbonyl)-2-azabicyclo[2.2.2]oct-2-yl]methanone
-
-
[(2R)-1-[N-(2,5-dichlorobenzoyl)glycyl]pyrrolidin-2-yl]boronic acid
-
-
Mn2+
-
93% residual activity at 0.2 mM
additional information
-
resistant to: PMSF, thyorphan, E64 and phosphoramidon
-
additional information
-
no effect by SH-reagents and metal chelators
-
additional information
-
comparison of inhibitory effects of methylchalcones on enzyme, trypsin and thrombin
-
additional information
-
the enzyme is completely resistant to digestion with pepsin
-
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
-
inhibitor synthesis, overview
-
additional information
-
inhibitor binding structure
-
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
-
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
-
additional information
-
not inhibited by carbamazepine, bupropion, diazepam, fluoxetine, haloperidol, lithium, maprotiline, mirtazapine, moclobemide, pargyline, pinoline, scopolamine, selegiline, sulpiride, venlafaxine, and valpraote at 0.01 mM concentration
-
additional information
-
not inhibited by cyclosporine A
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
endogenous inhibitor
-
additional information
-
-
-
additional information
-
-
-
additional information
-
different N-blocked L-proline-containing compounds and derivatives
-
additional information
-
not diisopropyl fluorophosphate, p-chloromercuriphenylsulfonic acid
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
2-mercaptoethanol
-
activation of the cytsolic isozyme, but not of the extracellular isozyme
3,4-dichloroisocoumarin
-
-
alpha-synuclein
plus interferon-gamma increases prolyl endopeptidase activity. Lipopolysaccharide, interferon-gamma or alpha-synuclein alone do not significantly upregulate prolyl endopeptidase enzymatic activity
-
dithiothreitol
up to 14fold stimulation
DTT
-
activation of the cytsolic isozyme, but not of the extracellular isozyme
DTT
in presence of DTT about 6fold higher catalytic efficiency of the enzyme
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
LPS
-
-
-
NaCl
-
slight activation
thiol reagents
-
activate
methotrexate
-
-
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
0.00042
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37C, 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, 37C, 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, 37C, 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, 37C, recombinant mutant C255T
0.00065
2-aminobenzoyl-FPQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C
3.7
2-aminobenzoyl-Glu-Gly-Phe-Ser-Pro-Phe(NO2)-Arg-Ala
-
-
1.32
2-aminobenzoyl-Glu-Phe-Ser-Pro-Phe(NO2)-Arg-Ala
-
-
6.3
2-aminobenzoyl-Gly-Glu-Ser-Pro-Phe(NO2)-Arg-Ala
-
-
0.4
2-aminobenzoyl-Gly-Phe-Arg-Pro-Phe(NO2)-Arg-Ala
-
-
1.54
2-aminobenzoyl-Gly-Phe-Glu-Pro-Phe(NO2)-Arg-Ala
-
-
0.00205
2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala-NH2
-
pH 8.0, wild-type enzyme
0.00024
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37C, recombinant wild-type enzyme
0.00033
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37C, 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, 37C, 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, 37C, 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, 37C, recombinant mutant C255T
0.00024
2-aminobenzoyl-Gly-Pro-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37C, recombinant wild-type enzyme
0.00036
2-aminobenzoyl-Gly-Pro-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37C, recombinant mutant C255T
0.00219
2-aminobenzoyl-Gly-Pro-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37C, recombinant wild-type enzyme
0.00141
2-aminobenzoyl-Gly-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37C, recombinant wild-type enzyme
0.00117
2-aminobenzoyl-Gly-Pro-Phe-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37C, recombinant wild-type enzyme
0.0019
2-aminobenzoyl-Gly-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
-
pH 7.5, 37C, recombinant wild-type enzyme
0.00074
2-aminobenzoyl-RPPGFSPFRQ-(N-(2,4-dinitrophenyl)ethylenediamine)
-
pH 8.0, 37C
1
7-succinyl-Gly-Pro-4-methylcoumarin 7-amide
-
-
-
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 25C
-
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 25C
-
0.35
Ala-Gly-Pro-beta-naphthylamide
Lyophyllum cinerascens
-
-
0.0194
Ala-Pro-4-nitroanilide
-
pH 7.5, 85C
0.0194
Ala-Pro-p-nitroanilide
-
pH 7.5, 85C
0.016
angiotensin I
-
-
0.036
angiotensin II
-
-
0.0229
Arg-Pro-4-nitroanilide
-
pH 7.5, 85C
0.16
Arg-Pro-4-nitroanilide
-
pH 7.5, 85C
0.0229
Arg-Pro-p-nitroanilide
-
pH 7.5, 85C
0.04
Asp-Pro-4-nitroanilide
-
pH 7.5, 85C
0.04
Asp-Pro-p-nitroanilide
-
pH 7.5, 85C
0.043
benzyloxycarbonyl-Ala-Ala-4-nitroanilide
-
pH 7.5, 85C
-
0.58
benzyloxycarbonyl-Ala-Ala-beta-naphthylamide
-
-
0.043
benzyloxycarbonyl-Ala-Ala-p-nitroanilide
-
pH 7.5, 85C
0.16
benzyloxycarbonyl-Ala-Ala-p-nitrophenol
-
-
0.29
benzyloxycarbonyl-Ala-Gly-Pro-beta-naphthylamide
-
-
0.31
benzyloxycarbonyl-Ala-Gly-Pro-beta-naphthylamide
Lyophyllum cinerascens
-
-
1.02
benzyloxycarbonyl-Ala-Gly-Pro-p-nitrophenol
-
enzyme from kidney
0.018
benzyloxycarbonyl-Ala-Pro-2-naphthylamide
-
-
0.0437
benzyloxycarbonyl-Ala-Pro-4-nitroanilide
-
pH 7.5, 85C
-
0.08
benzyloxycarbonyl-Ala-Pro-beta-naphthylamide
-
-
0.01
benzyloxycarbonyl-Ala-Pro-p-nitroanilide
Lyophyllum cinerascens
-
-
0.0437
benzyloxycarbonyl-Ala-Pro-p-nitroanilide
-
pH 7.5, 85C
0.07
benzyloxycarbonyl-Ala-Pro-p-nitrophenol
-
enzyme from kidney
0.14
benzyloxycarbonyl-D-Ala-Gly-Pro-beta-naphthylamide
-
-
1.67
benzyloxycarbonyl-D-Ala-Gly-Pro-beta-naphthylamide
Lyophyllum cinerascens
-
-
0.38
benzyloxycarbonyl-D-Ala-Gly-Pro-p-nitrophenol
-
enzyme from kidney
0.2
benzyloxycarbonyl-D-Ala-Pro-beta-naphthylamide
-
-
0.133
benzyloxycarbonyl-Gly-Gly-Pro-p-nitrophenol
-
-
0.27
benzyloxycarbonyl-Gly-Gly-Pro-p-nitrophenol
-
enzyme from kidney
0.06528
benzyloxycarbonyl-Gly-L-Pro-4-nitroanilide
-
in 25 mM ethanolamine, pH 8.5, at 20C
3.42
benzyloxycarbonyl-Gly-L-Pro-4-nitroanilide
-
at pH 8.0 and 37C
1.74
benzyloxycarbonyl-Gly-L-Pro-7-amido-4-methylcoumarin
-
at pH 8.0 and 37C
0.0014
benzyloxycarbonyl-Gly-L-Pro-beta-naphthylamide
-
pH 7.4, 37C, enzyme from thioglycollate-elicited macrophage
0.015
benzyloxycarbonyl-Gly-Pro-4-methylcoumarin 7-amide
-
-
0.02
benzyloxycarbonyl-Gly-Pro-4-methylcoumaryl-7-amide
Lyophyllum cinerascens
-
-
0.025
benzyloxycarbonyl-Gly-Pro-4-methylcoumaryl-7-amide
-
-
0.08
Benzyloxycarbonyl-Gly-Pro-Ala
-
enzyme from kidney
0.39
Benzyloxycarbonyl-Gly-Pro-Ala
-
-
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
0.02
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide
Lyophyllum cinerascens
-
-
0.14
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide
-
-
0.25
benzyloxycarbonyl-Gly-Pro-D-Ala
-
enzyme from kidney
0.32
benzyloxycarbonyl-Gly-Pro-D-Leu
-
enzyme from kidney
0.17
Benzyloxycarbonyl-Gly-Pro-Leu
-
enzyme from kidney
0.22
Benzyloxycarbonyl-Gly-Pro-Leu
-
-
0.12
benzyloxycarbonyl-Gly-Pro-Leu-Ala
-
enzyme from kidney
0.32
benzyloxycarbonyl-Gly-Pro-Leu-Ala
-
-
0.37
benzyloxycarbonyl-Gly-Pro-Leu-D-Ala
-
enzyme from kidney
1.5
benzyloxycarbonyl-Gly-Pro-Leu-D-Ala
-
-
0.06
Benzyloxycarbonyl-Gly-Pro-Leu-Gly
-
enzyme from kidney
0.47
Benzyloxycarbonyl-Gly-Pro-Leu-Gly
-
-
0.18
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Ala
-
enzyme from kidney
1.82
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Ala
-
-
0.14
benzyloxycarbonyl-Gly-Pro-Leu-Gly-D-Ala
-
enzyme from kidney
0.13
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Gly
-
enzyme from kidney
1.4
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Gly
-
-
0.68
Benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro
-
enzyme from kidney
0.16
benzyloxycarbonyl-Gly-Pro-p-nitroanilide
-
pH 7.5, 85C
0.4
benzyloxycarbonyl-Gly-Pro-p-nitroanilide
Lyophyllum cinerascens
-
-
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
0.07
benzyloxycarbonyl-Gly-Pro-p-nitrophenol
-
enzyme from kidney
0.125
benzyloxycarbonyl-Gly-Pro-p-nitrophenol
-
-
0.0192
benzyloxycarbonyl-Gly-Pro-p-nitrophenyl ester
-
pH 7.0, wild-type enzyme
0.16
Benzyloxycarbonyl-Gly-Pro-Phe
-
enzyme from kidney
0.74
Benzyloxycarbonyl-Gly-Pro-Phe
-
-
0.00152
benzyloxycarbonyl-Gly-Pro-SBzl
-
pH 7.0, mutant enzyme D641N
0.00159
benzyloxycarbonyl-Gly-Pro-SBzl
-
pH 7.0, mutant enzymeD641A
0.016
benzyloxycarbonyl-Gly-Pro-SBzl
-
pH 7.0, wild-type enzyme
0.14
benzyloxycarbonyl-Pro-p-nitrophenol
-
enzyme from kidney
0.0012
calcitonin gene-related peptide
-
mutant D35A/K196A, shorter peptide of calcitonin gene-related peptide
-
0.0034
calcitonin gene-related peptide
-
mutant D35A/K196A, diserine mutant of calcitonin gene-related peptide
-
0.0043
calcitonin gene-related peptide
-
wild type enzyme, full length calcitonin gene-related peptide
-
0.01
calcitonin gene-related peptide
-
wild type enzyme, shorter peptide of calcitonin gene-related peptide
-
0.0125
calcitonin gene-related peptide
-
wild type enzyme, diserine mutant of calcitonin gene-related peptide
-
0.6 - 2.4
furylacryloyl-Ala-Pro
-
-
0.0207
Gly-Pro-4-nitroanilide
-
pH 7.5, 85C
0.0207
Gly-Pro-p-nitroanilide
-
pH 7.5, 85C
0.18
L-Ala-L-Ala-L-Pro-4-nitroanilide
-
at pH 5.0 and 35C
0.16
N-benzyloxycarbonyl-Ala-Ala-p-nitrophenyl ester
-
-
0.48
N-benzyloxycarbonyl-Gly-Pro-Ala
-
-
0.06
N-benzyloxycarbonyl-Gly-Pro-Leu-Gly
-
-
0.125
N-benzyloxycarbonyl-Gly-Pro-p-nitrophenyl ester
-
-
0.029
N-carbobenzoxy-Gly-Pro-2-beta-naphthylamide
-
-
-
0.01521
N-Suc-Gly-Pro-Leu-Gly-Pro-7-amido-4-methylcoumarin
in absence of DTT
0.04413
N-Suc-Gly-Pro-Leu-Gly-Pro-7-amido-4-methylcoumarin
in presence of DTT
0.4
N-succinyl-Ala-Pro-4-nitroanilide
pH 7.5, 80C, recombinant enzyme
0.014
N-succinyl-Gly-L-Pro-L-Leu-Gly-L-Pro-7-amido-4-methylcoumarin
pH 7.5, native enzyme
0.0181
N-succinyl-Gly-L-Pro-L-Leu-Gly-L-Pro-7-amido-4-methylcoumarin
pH 7.5, recombinant enzyme
0.54
Nalpha-benzyloxycarbonyl-Gly-Pro-Leu-Gly
-
-
0.13
Vasopressin
-
-
0.26
Z-Gly-L-Pro-4-nitroanilide
-
at pH 5.0 and 35C
-
0.37
Z-Gly-L-Pro-4-nitroanilide
-
at 40C and pH 4.0
-
0.25
Z-Gly-Pro-4-nitroanilide
-
-
0.81
Z-Gly-Pro-4-nitroanilide
-
0.37
Z-L-Ala-L-Ala-L-Ala-L-Pro-4-nitroanilide
-
at pH 5.0 and 35C
-
0.56
Z-L-Ala-L-Ala-L-Ala-L-Pro-4-nitroanilide
-
at 40C and pH 4.0
-
0.28
L-Ala-L-Ala-L-Pro-4-nitroanilide
-
at 40C and pH 4.0
additional information
additional information
-
kinetics and substrate specificity, overview
-
additional information
additional information
-
kinetics and thermodynamics, and activation parameters, of full-length and truncated enzyme forms
-
additional information
additional information
-
kinetic and mechanistic studies
-
additional information
additional information
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additional information
additional information
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additional information
additional information
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additional information
additional information
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additional information
additional information
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additional information
additional information
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additional information
additional information
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additional information
additional information
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additional information
additional information
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additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
Sus scrofa
-
pH 7.5, 37C, recombinant mutant C255T
1.1
2-aminobenzoyl-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
Sus scrofa
-
pH 7.5, 37C, 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
Sus scrofa
-
pH 7.5, 37C, 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
Sus scrofa
-
pH 7.5, 37C, recombinant wild-type enzyme
0.03 - 0.55
2-aminobenzoyl-Glu-Gly-Phe-Ser-Pro-Phe(NO2)-Arg-Ala
Sus scrofa
-
-
7.22
2-aminobenzoyl-Glu-Gly-Phe-Ser-Pro-Phe(NO2)-Arg-Ala
Sus scrofa
-
-
1.7
2-aminobenzoyl-Glu-Phe-Ser-Pro-Phe(NO2)-Arg-Ala
Sus scrofa
-
-
1.82
2-aminobenzoyl-Gly-Glu-Ser-Pro-Phe(NO2)-Arg-Ala
Sus scrofa
-
-
2.94
2-aminobenzoyl-Gly-Glu-Ser-Pro-Phe(NO2)-Arg-Ala
Sus scrofa
-
-
3.2
2-aminobenzoyl-Gly-Phe-Arg-Pro-Phe(NO2)-Arg-Ala
Sus scrofa
-
-
2.4
2-aminobenzoyl-Gly-Phe-Glu-Pro-Phe(NO2)-Arg-Ala
Sus scrofa
-
-
3.3
2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala-NH2
Sus scrofa
-
pH 8.0, wild-type enzyme
5.38
2-aminobenzoyl-Gly-Phe-Gly-Pro-Phe-Gly-Phe(NO2)-Ala-NH2
Sus scrofa
-
pH 8.0, wild-type enzyme
1.4
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
Sus scrofa
-
pH 7.5, 37C, recombinant wild-type enzyme
1.4
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
Sus scrofa
-
pH 7.5, 37C, recombinant mutant C255T
1.5
2-aminobenzoyl-Gly-Phe-Ser-Pro-Phe-Arg-Ser-Ser-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
Sus scrofa
-
pH 7.5, 37C, recombinant wild-type enzyme
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
Sus scrofa
-
pH 7.5, 37C, recombinant wild-type enzyme and mutant C255T
1.4
2-aminobenzoyl-Gly-Pro-Gln-N-(2,4-dinitrophenyl)ethylenediamine
Sus scrofa
-
pH 7.5, 37C, recombinant wild-type enzyme
1.8
2-aminobenzoyl-Gly-Pro-Gln-N-(2,4-dinitrophenyl)ethylenediamine
Sus scrofa
-
pH 7.5, 37C, recombinant mutant C255T
7.9
2-aminobenzoyl-Gly-Pro-Gln-N-(2,4-dinitrophenyl)ethylenediamine
Sus scrofa
-
pH 7.5, 37C, recombinant wild-type enzyme
4
2-aminobenzoyl-Gly-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
Sus scrofa
-
pH 7.5, 37C, recombinant wild-type enzyme
6
2-aminobenzoyl-Gly-Pro-Phe-Gln-N-(2,4-dinitrophenyl)ethylenediamine
Sus scrofa
-
pH 7.5, 37C, recombinant wild-type enzyme
3.5
2-aminobenzoyl-Gly-Ser-Pro-Phe-Arg-Gln-N-(2,4-dinitrophenyl)ethylenediamine
Sus scrofa
-
pH 7.5, 37C, recombinant wild-type enzyme
0.97
Abz-Gly-L-Phe-L-Arg-L-Pro-L-Phe(NO2)-L-Arg-L-Ala
Homo sapiens
-
wild type enzyme, at pH 8.0 and 25C
-
1.31
Abz-Gly-L-Phe-L-Arg-L-Pro-L-Phe(NO2)-L-Arg-L-Ala
Homo sapiens
-
mutant enzyme T202C/T590C, at pH 8.0 and 25C
-
15.9
Ala-Gly-Pro-beta-naphthylamide
Lyophyllum cinerascens
-
-
0.079
Ala-Pro-4-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
0.079
Ala-Pro-p-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
0.85
angiotensin I
Bos taurus
-
-
0.03
Arg-Pro-4-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
16.9
Arg-Pro-4-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
0.03
Arg-Pro-p-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
0.073
Asp-Pro-4-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
0.073
Asp-Pro-p-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
2.5
benzyloxycarbonyl-Ala-Ala-4-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
-
5.9
benzyloxycarbonyl-Ala-Ala-beta-naphthylamide
Elizabethkingia meningoseptica
-
-
2.5
benzyloxycarbonyl-Ala-Ala-p-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
2.7
benzyloxycarbonyl-Ala-Ala-p-nitrophenol
Elizabethkingia meningoseptica
-
-
0.82
benzyloxycarbonyl-Ala-Gly-Pro-beta-naphthylamide
Lyophyllum cinerascens
-
-
192
benzyloxycarbonyl-Ala-Gly-Pro-beta-naphthylamide
Elizabethkingia meningoseptica
-
-
38.2
benzyloxycarbonyl-Ala-Gly-Pro-p-nitrophenol
Ovis aries
-
enzyme from kidney
17.9
benzyloxycarbonyl-Ala-Pro-4-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
-
4.2
benzyloxycarbonyl-Ala-Pro-beta-naphthylamide
Elizabethkingia meningoseptica
-
-
17.9
benzyloxycarbonyl-Ala-Pro-p-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
126
benzyloxycarbonyl-Ala-Pro-p-nitroanilide
Lyophyllum cinerascens
-
-
61
benzyloxycarbonyl-Ala-Pro-p-nitrophenol
Ovis aries
-
enzyme from kidney
2
benzyloxycarbonyl-D-Ala-Gly-Pro-beta-naphthylamide
Lyophyllum cinerascens
-
-
38
benzyloxycarbonyl-D-Ala-Gly-Pro-beta-naphthylamide
Elizabethkingia meningoseptica
-
-
30
benzyloxycarbonyl-D-Ala-Gly-Pro-p-nitrophenol
Ovis aries
-
enzyme from kidney
0.147
benzyloxycarbonyl-D-Ala-Pro-beta-naphthylamide
Elizabethkingia meningoseptica
-
-
2.05
benzyloxycarbonyl-Gly-Gly-Pro-p-nitrophenol
Elizabethkingia meningoseptica
-
-
27
benzyloxycarbonyl-Gly-Gly-Pro-p-nitrophenol
Ovis aries
-
enzyme from kidney
85.8
benzyloxycarbonyl-Gly-Gly-Pro-p-nitrophenol
Elizabethkingia meningoseptica
-
-
162
benzyloxycarbonyl-Gly-L-Pro-4-nitroanilide
Coprinopsis clastophylla
-
at pH 8.0 and 37C
26.6
benzyloxycarbonyl-Gly-L-Pro-7-amido-4-methylcoumarin
Coprinopsis clastophylla
-
at pH 8.0 and 37C
4.7
benzyloxycarbonyl-Gly-L-Pro-beta-naphthylamide
Mus musculus
-
pH 7.4, 37C, enzyme from thioglycollate-elicited macrophage
0.95
benzyloxycarbonyl-Gly-Pro-4-methylcoumaryl-7-amide
Lyophyllum cinerascens
-
-
115
benzyloxycarbonyl-Gly-Pro-4-methylcoumaryl-7-amide
Elizabethkingia meningoseptica
-
-
1.26
Benzyloxycarbonyl-Gly-Pro-Ala
Lyophyllum cinerascens
-
-
6.08
Benzyloxycarbonyl-Gly-Pro-Ala
Lyophyllum cinerascens
-
-
15.6
Benzyloxycarbonyl-Gly-Pro-Ala
Ovis aries
-
enzyme from kidney
240
Benzyloxycarbonyl-Gly-Pro-Ala
Elizabethkingia meningoseptica
-
-
0.0151
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide
Sus scrofa
-
pH 7.0, mutant enzyme D641N
0.0657
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide
Sus scrofa
-
pH 7.0, mutant enzyme D641A
32.5
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide
Sus scrofa
-
pH 7.0, wild-type enzyme
153
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide
Lyophyllum cinerascens
-
-
169
benzyloxycarbonyl-Gly-Pro-beta-naphthylamide
Elizabethkingia meningoseptica
-
-
1.52
benzyloxycarbonyl-Gly-Pro-D-Ala
Ovis aries
-
enzyme from kidney
2.94
benzyloxycarbonyl-Gly-Pro-D-Ala
Ovis aries
-
enzyme from kidney
0.67
benzyloxycarbonyl-Gly-Pro-D-Leu
Ovis aries
-
enzyme from kidney
6.08
benzyloxycarbonyl-Gly-Pro-D-Leu
Ovis aries
-
enzyme from kidney
1.05
Benzyloxycarbonyl-Gly-Pro-Leu
Lyophyllum cinerascens
-
-
23
Benzyloxycarbonyl-Gly-Pro-Leu
Elizabethkingia meningoseptica
-
-
26
Benzyloxycarbonyl-Gly-Pro-Leu
Ovis aries
-
enzyme from kidney
13.2
benzyloxycarbonyl-Gly-Pro-Leu-Ala
Lyophyllum cinerascens
-
-
38.4
benzyloxycarbonyl-Gly-Pro-Leu-Ala
Ovis aries
-
enzyme from kidney
5.67
benzyloxycarbonyl-Gly-Pro-Leu-D-Ala
Lyophyllum cinerascens
-
-
46
benzyloxycarbonyl-Gly-Pro-Leu-D-Ala
Ovis aries
-
enzyme from kidney
1600
benzyloxycarbonyl-Gly-Pro-Leu-D-Ala
Elizabethkingia meningoseptica
-
-
0.031 - 0.51
Benzyloxycarbonyl-Gly-Pro-Leu-Gly
Lyophyllum cinerascens
-
-
7.98
Benzyloxycarbonyl-Gly-Pro-Leu-Gly
Lyophyllum cinerascens
-
-
52
Benzyloxycarbonyl-Gly-Pro-Leu-Gly
Ovis aries
-
enzyme from kidney
520
Benzyloxycarbonyl-Gly-Pro-Leu-Gly
Elizabethkingia meningoseptica
-
-
34
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Ala
Ovis aries
-
enzyme from kidney
1000
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Ala
Elizabethkingia meningoseptica
-
-
25
benzyloxycarbonyl-Gly-Pro-Leu-Gly-D-Ala
Ovis aries
-
enzyme from kidney
2 - 8
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Gly
Ovis aries
-
enzyme from kidney
700
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Gly
Elizabethkingia meningoseptica
-
-
0.4
Benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro
Ovis aries
-
enzyme from kidney
12.4
Benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro
Lyophyllum cinerascens
-
-
53.3
Benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro
Ovis aries
-
enzyme from kidney
3.8
benzyloxycarbonyl-Gly-Pro-p-nitroanilide
Lyophyllum cinerascens
-
-
16.9
benzyloxycarbonyl-Gly-Pro-p-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
0.021
benzyloxycarbonyl-Gly-Pro-p-nitrophenol
Sus scrofa
-
pH 7.0, mutant enzyme D641N
0.031
benzyloxycarbonyl-Gly-Pro-p-nitrophenol
Sus scrofa
-
pH 7.0, mutant enzyme D641A
3 - 6
benzyloxycarbonyl-Gly-Pro-p-nitrophenol
Sus scrofa
-
pH 7.0, wild-type enzyme
32.7
benzyloxycarbonyl-Gly-Pro-p-nitrophenol
Ovis aries
-
enzyme from kidney
102
benzyloxycarbonyl-Gly-Pro-p-nitrophenol
Elizabethkingia meningoseptica
-
-
3.2
Benzyloxycarbonyl-Gly-Pro-Phe
Ovis aries
-
enzyme from kidney
3.95
Benzyloxycarbonyl-Gly-Pro-Phe
Lyophyllum cinerascens
-
-
180
Benzyloxycarbonyl-Gly-Pro-Phe
Elizabethkingia meningoseptica
-
-
0.028
benzyloxycarbonyl-Gly-Pro-SBzl
Sus scrofa
-
pH 7.0, mutante enzyme D641N
0.099
benzyloxycarbonyl-Gly-Pro-SBzl
Sus scrofa
-
pH 7.0, mutant enzymeD641A
108
benzyloxycarbonyl-Gly-Pro-SBzl
Sus scrofa
-
pH 7.0, wild-type enzyme
8.9
benzyloxycarbonyl-Pro-p-nitrophenol
Ovis aries
-
enzyme from kidney
0.0012
calcitonin gene-related peptide
Mus musculus
-
wild type enzyme, full length calcitonin gene-related peptide
-
0.002
calcitonin gene-related peptide
Mus musculus
-
wild type enzyme, diserine mutant of calcitonin gene-related peptide
-
0.0023
calcitonin gene-related peptide
Mus musculus
-
mutant D35A/K196A, diserine mutant of calcitonin gene-related peptide
-
0.0051
calcitonin gene-related peptide
Mus musculus
-
mutant D35A/K196A, shorter peptide of calcitonin gene-related peptide
-
0.072
calcitonin gene-related peptide
Mus musculus
-
wild type enzyme, shorter peptide of calcitonin gene-related peptide
-
0.06
Gly-Pro-4-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
0.06
Gly-Pro-p-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
107.4
L-Ala-L-Ala-L-Pro-4-nitroanilide
Aspergillus oryzae
-
at pH 5.0 and 35C
6.1
N-benzyloxycarbonyl-Gly-Pro-Ala
Ovis aries
-
-
32.3
N-benzyloxycarbonyl-Gly-Pro-Leu-Gly
Ovis aries
-
-
22.2
N-succinyl-Ala-Pro-4-nitroanilide
Thermococcus onnurineus
Q2QC90
pH 7.5, 80C, recombinant enzyme
28.1
N-succinyl-Gly-L-Pro-L-Leu-Gly-L-Pro-7-amido-4-methylcoumarin
Trypanosoma cruzi
Q71MD6
pH 7.5, native enzyme
48.7
N-succinyl-Gly-L-Pro-L-Leu-Gly-L-Pro-7-amido-4-methylcoumarin
Trypanosoma cruzi
Q71MD6
pH 7.5, recombinant enzyme
29.2
Nalpha-benzyl-Gly-Pro-Leu-Gly
Elizabethkingia meningoseptica
-
-
17.6
Nalpha-benzyloxycarbonyl-Gly-Pro-Leu-Gly
Elizabethkingia meningoseptica
-
-
14.4
thyrotropin-releasing hormone
Bos taurus
-
-
105.7
Z-Gly-L-Pro-4-nitroanilide
Aspergillus oryzae
-
at 40C and pH 4.0
-
240
Z-Gly-L-Pro-4-nitroanilide
Aspergillus oryzae
-
at pH 5.0 and 35C
-
505
Z-Gly-Pro-4-nitroanilide
Aeromonas caviae
Q9X6R4
-
75
Z-L-Ala-L-Ala-L-Ala-L-Pro-4-nitroanilide
Aspergillus oryzae
-
at pH 5.0 and 35C
-
93
Z-L-Ala-L-Ala-L-Ala-L-Pro-4-nitroanilide
Aspergillus oryzae
-
at 40C and pH 4.0
-
520
benzyloxycarbonyl-Gly-Pro-Leu-Ala
Elizabethkingia meningoseptica
-
-
additional information
benzyloxycarbonyl-Gly-Pro-Leu-D-Ala
Lyophyllum cinerascens
-
-
139.4
L-Ala-L-Ala-L-Pro-4-nitroanilide
Aspergillus oryzae
-
at 40C and pH 4.0
additional information
additional information
Pyrococcus furiosus
-
kinetic and mechanistic studies
-
additional information
additional information
Ovis aries
-
-
-
additional information
additional information
Elizabethkingia meningoseptica
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.08
Ala-Pro-4-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
6622
1.31
Arg-Pro-4-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
8047
106
Arg-Pro-4-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
8047
1.82
Asp-Pro-4-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
20663
57.6
benzyloxycarbonyl-Ala-Ala-4-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
42481
410
benzyloxycarbonyl-Ala-Pro-4-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
42480
47.4
benzyloxycarbonyl-Gly-L-Pro-4-nitroanilide
Coprinopsis clastophylla
-
at pH 8.0 and 37C
36158
15.1
benzyloxycarbonyl-Gly-L-Pro-7-amido-4-methylcoumarin
Coprinopsis clastophylla
-
at pH 8.0 and 37C
59661
0.16
calcitonin gene-related peptide
Mus musculus
-
wild type enzyme, diserine mutant of calcitonin gene-related peptide
5834
0.22
calcitonin gene-related peptide
Mus musculus
-
mutant D35A/K196A, full length calcitonin gene-related peptide
5834
0.28
calcitonin gene-related peptide
Mus musculus
-
wild type enzyme, full length calcitonin gene-related peptide
5834
0.66
calcitonin gene-related peptide
Mus musculus
-
mutant D35A/K196A, diserine mutant of calcitonin gene-related peptide
5834
4.3
calcitonin gene-related peptide
Mus musculus
-
mutant D35A/K196A, shorter peptide of calcitonin gene-related peptide
5834
6.9
calcitonin gene-related peptide
Mus musculus
-
wild type enzyme, shorter peptide of calcitonin gene-related peptide
5834
2.9
Gly-Pro-4-nitroanilide
Pyrococcus furiosus
-
pH 7.5, 85C
1115
496.4
L-Ala-L-Ala-L-Pro-4-nitroanilide
Aspergillus oryzae
-
at 40C and pH 4.0
133491
33
N-Suc-Gly-Pro-Leu-Gly-Pro-7-amido-4-methylcoumarin
Trypanosoma brucei brucei
Q6HA27
in absence of DTT
40536
209
N-Suc-Gly-Pro-Leu-Gly-Pro-7-amido-4-methylcoumarin
Trypanosoma brucei brucei
Q6HA27
in presence of DTT
40536
24
Z-Gly-L-Pro-4-nitroanilide
Aspergillus oryzae
-
at pH 5.0 and 35C
148651
285.7
Z-Gly-L-Pro-4-nitroanilide
Aspergillus oryzae
-
at 40C and pH 4.0
148651
623
Z-Gly-Pro-4-nitroanilide
Aeromonas caviae
Q9X6R4
-
14731
166.1
Z-L-Ala-L-Ala-L-Ala-L-Pro-4-nitroanilide
Aspergillus oryzae
-
at 40C and pH 4.0
202347
202.7
Z-L-Ala-L-Ala-L-Ala-L-Pro-4-nitroanilide
Aspergillus oryzae
-
at pH 5.0 and 35C
202347
596.7
L-Ala-L-Ala-L-Pro-4-nitroanilide
Aspergillus oryzae
-
at pH 5.0 and 35C
133491
additional information
additional information
Pyrococcus furiosus
-
kinetic and mechanistic studies
2
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00087
((8'Z)-pentadecenyl)-salicylic acid
-
-
0.00000036
(2S)-1-[1-(3-[[(2S)-2-(cyclopentylcarbonyl)pyrrolidin-1-yl]carbonyl]benzoyl)-L-prolyl]pyrrolidine-2-carbonitrile
-
brain
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, 23C
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, 23C
0.0000118
(2S,2'S)-1,1'-(benzene-1,3-diyldicarbonyl)bis[2-(pyrrolidin-1-ylcarbonyl)pyrrolidine]
-
pH 7.0, 23C
0.0000272
1,2,3,4,6-pentagalloyl glucopyranoside
-
-
0.000405
1,2,3,6-tetragalloyl alloside
-
-
0.00249
1,2,3-trigalloyl glucopyranoside
-
-
0.000203
1,2,6-trigalloyl alloside
-
-
0.0000194
1,2,6-trigalloyl glucopyranoside
-
-
0.000194
1,2,6-trigalloyl glucopyranoside
-
-
0.0000004
1,3,6-trigalloyl alloside
-
-
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, 23C
5
4-(2-aminoethyl)-benzenesulfonyl fluoride
-
pH 7.5, 85C
0.0000042
4-(4-[123I]iodophenyl)butanoyl-L-prolyl-2(S)-cyanopyrrolidine
-
pH and temperature not specified in the publication
-
0.000000026
4-phenylbutanoyl-5(R)-methyl-L-Pro-2(S)-(hydroxyacetyl)pyrrolidine
-
pH 7.0, 30C
0.000000022
4-phenylbutanoyl-5(R)-t-butyl-L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine
-
pH 7.0, 23C
0.00000039
4-phenylbutanoyl-5(R)-t-butyl-L-prolyl-pyrrolidine
-
pH 7.0, 23C
0.000000015
4-phenylbutanoyl-5(R)-tert-butyl-L-Pro-2(S)-(hydroxyacetyl)-pyrrolidine
-
pH 7.0, 30C
0.000000015
4-phenylbutanoyl-5(R)-tert-butyl-L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine
-
at 25C between pH 5.5 and 9.5
-
0.000000018
4-phenylbutanoyl-L-Pro-2(S)-(hydroxyacetyl)-pyrrolidine
-
pH 7.0, 30C
0.00000002
4-phenylbutanoyl-L-prolyl-2(S)-cyanopyrrolidine
-
at 25C between pH 5.5 and 9.5
-
0.000000023
4-phenylbutanoyl-L-prolyl-2(S)cyanopyrrolidine
-
pH 7.0, 23C
0.00000097
4-phenylbutanoyl-L-prolyl-pyrrolidine
-
pH 7.0, 23C
0.0008
6-((10'Z)-heptadecenyl)salicylic acid
-
-
0.0008
6-(10Z-heptadecenyl)salicylic acid
-
pH 7.0, 37C
0.00087
6-(8Z-pentadecenyl)salicylic acid
-
pH 7.0, 37C
0.000033
9H-fluoren-9-ylmethyl [(2S)-5-carbamimidamido-1-[(2S)-2-cyanopyrrolidin-1-yl]-1-oxopentan-2-yl]carbamate
-
brain
0.000074
acetonyl geraniin
-
-
0.0913
arachidonic acid
-
37C, pH 7.0
0.00000073
ARI-3099
-
at 25C, pH not specified in the publication
-
0.0000031
ARI-3531
-
at 25C, pH not specified in the publication
-
0.000003
benzyl (1S,2S)-2-[[(2S)-2-formylpyrrolidin-1-yl]carbonyl]cyclohexanecarboxylate
-
brain
0.00161
benzyl (2S)-2-[(1-oxido-1,3-thiazolidin-3-yl)carbonyl]pyrrolidine-1-carboxylate
-
brain
0.042
benzyl (2S)-2-[[(2S)-2-(hydroxymethyl)pyrrolidin-1-yl]carbonyl]pyrrolidine-1-carboxylate
-
brain
0.0000024
benzyl (2S)-2-[[(2S)-2-formylpyrrolidin-1-yl]carbonyl]-2,3-dihydro-1H-indole-1-carboxylate
-
brain
0.00000035
benzyl (2S)-2-[[(2S)-2-formylpyrrolidin-1-yl]carbonyl]pyrrolidine-1-carboxylate
-
brain
0.0000005
benzyl (2S)-2-[[(2S)-2-formylpyrrolidin-1-yl]carbonyl]pyrrolidine-1-carboxylate
-
-
0.000014
benzyl (2S)-2-[[(2S)-2-formylpyrrolidin-1-yl]carbonyl]pyrrolidine-1-carboxylate
-
brain
0.0002
benzyl [(3R,6R,7aS)-3-cyano-5-oxohexahydropyrrolo[2,1-b][1,3]thiazol-6-yl]carbamate
-
human brain
0.07
benzyl [2-[(2S)-2-(chloroacetyl)pyrrolidin-1-yl]-2-oxoethyl]carbamate
-
brain
0.000000055
benzylcarbamoyl-L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine
-
at 25C between pH 5.5 and 9.5
-
0.00000035
benzyloxycarbonyl-Pro-prolinal
-
-
0.000212
corilagin
-
-
0.00000015
cyclopent-2-ene-1,2-dicarboxylic acid 2-benzylamide 1-[2(S)-(hydroxyacetyl)-H-pyrrolidine]amide
-
at 25C between pH 5.5 and 9.5
-
0.089
docosahexaenoic acid
-
37C, pH 7.0
0.2475
eicosapentaenoic acid
-
37C, pH 7.0
0.0000184
elaeocarpusin
-
-
0.0000046
euphorscopin
-
-
0.0000171
geraniin
-
-
0.000129
helioscopin B
-
-
0.000102
helioscopinin A
-
-
0.000098
helioscopinin B
-
-
0.000000048
isophthalic acid 2(S)-(cyclopentanecarbonyl)pyrrolidine-L-prolyl-2(S)-(hydroxyacetyl)pyrrolidine amide
-
pH 7.0, 23C
0.00000036
isophthalic acid 2(S)-(cyclopentanecarbonyl)pyrrolidine-L-prolyl-2(S)-cyanopyrrolidine amide
-
pH 7.0, 23C
0.00079
jolkinin
-
-
0.00000083
JTP-4819
-
-
0.000000023
KYP-2047
-
pH and temperature not specified in the publication
0.051
linoleic acid
-
37C, pH 7.0
0.278
N-succinyl-Gly-Pro-OH
-
-
0.0267
oleic acid
-
37C, pH 7.0
0.000012
ONO-1603
-
-
0.000012
ONO-1603
-
rat cortex
0.00000026
phenyl (2S)-2-(((2S)-2-(1,3-thiazol-2-ylcarbonyl)pyrrolidin-1-yl)carbonyl)pyrrolidine-1-carboxylate
pH 7.5, native enzyme
0.0000009
phenyl (2S)-2-(((2S)-2-(1,3-thiazol-2-ylcarbonyl)pyrrolidin-1-yl)carbonyl)pyrrolidine-1-carboxylate
pH 7.5, recombinant enzyme
0.000072
phenyl (2S)-2-(((2S)-2-(isoxazol-3-ylcarbonyl)pyrrolidin-yl)carbonyl)pyrrolidine-1-carboxylate
pH 7.5, native enzyme
0.000083
phenyl (2S)-2-(((2S)-2-(isoxazol-3-ylcarbonyl)pyrrolidin-yl)carbonyl)pyrrolidine-1-carboxylate
pH 7.5, recombinant enzyme
0.00000021
phenyl (2S)-2-([(2S)-2-[(5-phenylisoxazol-3-yl)carbonyl]pyrrolidin-1-yl]carbonyl)pyrrolidine-1-carboxylate
pH 7.5, native enzyme
0.00000048
phenyl (2S)-2-([(2S)-2-[(5-phenylisoxazol-3-yl)carbonyl]pyrrolidin-1-yl]carbonyl)pyrrolidine-1-carboxylate
pH 7.5, recombinant enzyme
0.00000028
phenyl (2S)-2-[[(2S)-2-([5-[(2E)-3-phenylprop-2-en-1-yl]isoxazol-3-yl]carbonyl)pyrrolidin-1-yl]carbonyl]pyrrolidine-1-carboxylate
pH 7.5, native enzyme
0.0000008
phenyl (2S)-2-[[(2S)-2-([5-[(2E)-3-phenylprop-2-en-1-yl]isoxazol-3-yl]carbonyl)pyrrolidin-1-yl]carbonyl]pyrrolidine-1-carboxylate
pH 7.5, recombinant enzyme
0.00000045
phenyl (2S)-2-[[(2S)-2-[[5-(trimethylsilyl)isoxazol-3-yl]carbonyl]pyrrolidin-1-yl]carbonyl]pyrrolidine-1-carboxylate
pH 7.5, native enzyme
0.0000015
phenyl (2S)-2-[[(2S)-2-[[5-(trimethylsilyl)isoxazol-3-yl]carbonyl]pyrrolidin-1-yl]carbonyl]pyrrolidine-1-carboxylate
pH 7.5, recombinant enzyme
0.0000094
rugosin E
-
-
0.000001
S 17092
-
extracellular enzyme
0.00003
S 17092
-
intracellular enzyme
0.0000015
S-17092
-
-
0.0000072
SUAM-1221
-
-
0.000091
supinanin
-
-
0.311
tasidotin
-
chromogenic assay
0.42
tasidotin
-
fluorogenic assay
0.001717
teracatain
-
-
0.00554
tert-butyl [(2S)-3-methyl-1-(1,3-thiazolidin-3-yl)-1-thioxobutan-2-yl]carbamate
-
human placenta
0.00000095
Y-29794
-
rat cortex
0.0000002
Z-Pro-prolinal
-
at 25C between pH 5.5 and 9.5
0.0029
ZTTA
-
rat brain
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
-
-
0.0029
benzyl (2S)-2-(1,3-oxazolidin-3-ylcarbonyl)pyrrolidine-1-carboxylate
-
brain
additional information
benzyl (2S)-2-(1,3-thiazolidin-3-ylcarbonyl)pyrrolidine-1-carboxylate
-
brain, value between 39 and 110 nM
additional information
benzyl (2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidine-1-carboxylate
-
brain, value between 0.0021 and 0.0024 mM
0.0000034
benzyl (2S)-2-[[(2S)-2-formylpyrrolidin-1-yl]carbonyl]-5-oxopyrrolidine-1-carboxylate
-
brain
additional information
benzyl (2S)-2-[[(2S)-2-formylpyrrolidin-1-yl]carbonyl]pyrrolidine-1-carboxylate
-
brain, value between 0.21 and 5 nM
0.000441
macranganin
-
-
additional information
additional information
-
inhibition kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000109
(+)-gallocatechin
Elizabethkingia meningoseptica
-
IC50: 0.000109 mM, expected to be useful for preventing and curing of Alzheimers disease
0.0281
(-)-epicatechin
Elizabethkingia meningoseptica
-
IC50: 0.0281 mM, noncompetitive inhibition
10.2
(-)-epicatechin gallate
Elizabethkingia meningoseptica
-
IC50: 10.2 mM, expected to be useful for preventing and curing of Alzheimers disease
0.000142
(-)-epigallocatechin gallate
Elizabethkingia meningoseptica
-
IC50: 0.000142 mM, expected to be useful for preventing and curing of Alzheimers disease
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
0.00003
(2S)-1-(4-phenylbutanoyl)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidine
Sus scrofa
-
-
0.000048
(2S)-1-octanoyl-2-(pyrrolidin-1-ylcarbonyl)pyrrolidine
Sus scrofa
-
-
0.00000045
(2S)-1-[1-(2,3-dihydro-1H-inden-2-ylacetyl)-L-prolyl]pyrrolidine-2-carbaldehyde
Canis lupus familiaris
-
brain
0.0000012
(2S)-1-[1-(2,3-dihydro-1H-inden-2-ylacetyl)-L-prolyl]pyrrolidine-2-carbonitrile
Canis lupus familiaris
-
brain
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
-
-
0.000002
(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
-
-
0.000002
(3S)-N-benzyl-3-[[(2S)-2-(chloroacetyl)pyrrolidin-1-yl]carbonyl]-3,4-dihydroisoquinoline-2(1H)-carboxamide
Trypanosoma brucei brucei
Q6HA27
-
0.000011
(4R)-3-octanoyl-4-(pyrrolidin-1-ylcarbonyl)-1,3-thiazolidine
Sus scrofa
-
-
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
-
-