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Information on EC 3.4.21.26 - prolyl oligopeptidase and Organism(s) Rattus norvegicus and UniProt Accession O70196
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3.4.21.26 prolyl oligopeptidaseSpecify your search results
Word Map
- 3.4.21.26
-
dipeptidyl
-
stroma
-
cancer-associated
- aminopeptidase
- neuropeptides
- endopeptidases
- neurotensin
-
proline-containing
-
fapis
-
biodistribution
-
myofibroblasts
- flavobacterium
- celiac
-
beta-propeller
- bradykinin
- trh
- dppiv
- meningosepticum
-
3.4.14.5
-
18f-fdg
-
theranostic
-
exopeptidase
-
pyroglutamyl
- phosphoramidon
- amanita
- amnesia
-
carcinoma-associated
-
peptidase-iv
- pharmacology
-
ac-sdkp
-
seven-bladed
-
gluten-free
-
suvmean
- gliadin
-
n-acetyl-seryl-aspartyl-lysyl-proline
-
bispecific
-
acylpeptide
- medicine
- nutrition
- food industry
- drug development
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
prolyl oligopeptidase, fibroblast activation protein, proline endopeptidase, post-proline cleaving enzyme, prolylendopeptidase, proline-specific endopeptidase, post-proline endopeptidase, glutenase, prolyl endoprotease, pepo2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
endoprolylpeptidase
-
-
-
-
peptidase, postproline endo-
-
-
-
-
POP
-
-
post-proline cleaving enzyme
post-proline endopeptidase
-
-
-
-
postproline endopeptidase
-
-
-
-
postproline-cleaving enzyme
-
-
-
-
proline endopeptidase
-
-
-
-
proline-specific endopeptidase
-
-
-
-
prolyl endopeptidase
additional information
-
the enzyme belongs to the POP family of serine proteases, family S9 of clan SC
post-proline cleaving enzyme
-
-
-
-
prolyl endopeptidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
catalytic mechanism, structure-function relationship
-
Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides
the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY
72162-84-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-benzyl 2-(2-(4-hydroxynaphthalen-1-ylcarbamoyl)pyrrolidin-1-yl)-2-oxoethylcarbamate + H2O
?
-
specific substrate, UAMC-00682
-
-
?
benzyloxycarbonyl-Gly-Pro-2-naphthylamide + H2O
benzyloxycarbonyl-Gly-Pro + 2-naphthylamine
-
-
-
?
N-carbobenzyloxy-Ala-Pro-2-naphthylamide + H2O
N-carbobenzyloxy-Ala-Pro + 2-naphthylamine
-
-
-
-
?
N-succinyl-glycyl-proline-4-methylcoumarin-7-amide + H2O
N-succinyl-glycyl-proline + 7-amino-4-methylcoumarin
-
-
-
-
?
N-succinyl-glycyl-prolyl-7-amido-4-methylcoumarin + H2O
N-succinyl-glycyl-prolyl + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
succinyl-Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
thymosin beta4 + H2O
acetyl-N-Ser-Asp-Lys-Pro + ?
-
prolyl oligopeptidase is a second-step enzyme in the release of acetyl-N-Ser-Asp-Lys-Pro from thymosin beta4 and has autoregulatory effect in the first step
-
-
?
additional information
?
-
prolyl oligopeptidase binds to the growth-38 associated protein GAP-43, which is a key regulator of synaptic plasticity
-
-
?
additional information
?
-
-
tissue-dependent peptide hydrolysis evoked by prolyl endopeptidase activity is involved in the water-electrolyte homeostasis
-
?
additional information
?
-
-
cellular functions, overview, POP may regulate phosphoinositide signaling, overview
-
-
?
additional information
?
-
-
the enzyme in the brain dopaminergix system is involved in the pathogenesis of doamine deficiency-dependent depressive states, and is activated in association with development of MPTP-induced depressive syndrome in the brain frontal cortex, overview
-
-
?
additional information
?
-
-
the enzyme is a serine protease, that digests small peptide-like hormones, neuroactive peptides, and various cellular factors, it is implicated in several biological processes and diseases, e.g. in some psychiatric disorders, most probably through interference in the inositol cycle, it is important in the metabolism of substance P, arginine vasopressin, thyroliberin, and gonadoliberin, enzyme regulation, overview
-
-
?
additional information
?
-
-
the enzyme is associated with cognitive functions and inositol 1,4,5-triphosphate signaling, and plays a role in modifying neuropeptide levels, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the phosphoinositide pathway, in formation and processing of amyloid beta-peptide, protein secretion, and in neuronal differentiation and maturation, overview, the enzyme is involved in several diseases, e.g. celiac disease, Alzheimer's diease, Parkinsons's disease, affective disorders, eating disorders, cancer, inflammation, hypertension, and neurodegenarative disorders, overview, enzyme inhibition can improve the retention time when administered before either the acquisition or the retential trial in scopolamine-induced amnesia, enzyme inhibition also positively affects neurodiseases, overview
-
-
?
additional information
?
-
-
the enzyme is involved with the inactivation of regulatory neuropeptides
-
-
?
additional information
?
-
-
the enzyme plays a role in inositol 1,4,5-triphosphate signaling and in the actions of antidepressants, POP inhibitors have antiamnesic and neuroprotective properties, overview
-
-
?
additional information
?
-
-
no activity with gluten in celiac sprue rats, substrate specificity with exclusion of peptides with more than 30 amino acids, overview
-
-
?
additional information
?
-
-
substrate specificity, overview, the enzyme cleaves at the C-terminal side of proline residues and more slowly of alanine residues, no activity with large proteins with over 30 amino acids
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme shows endopeptidase activity with peptides no longer than 3 amino acids
-
-
?
additional information
?
-
-
the serine protease cleaves at the C-terminal side of proline residues and more slowly of alanine residues of peptides with no more than 30 amino acids
-
-
?
additional information
?
-
-
hydrolyzes proline-containing peptides shorter than 30 amino acids
-
-
?
additional information
?
-
-
is involved in thalamocortical and corticothalamic signal processing
-
-
?
additional information
?
-
-
the recombinant prolyl oligopeptidase is not able to cleave whole 43-mer thymosin beta4, while it is effective at hydrolyzing somatostatin-28 (1-12)
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
prolyl oligopeptidase binds to the growth-38 associated protein GAP-43, which is a key regulator of synaptic plasticity
-
-
?
additional information
?
-
-
tissue-dependent peptide hydrolysis evoked by prolyl endopeptidase activity is involved in the water-electrolyte homeostasis
-
?
additional information
?
-
-
cellular functions, overview, POP may regulate phosphoinositide signaling, overview
-
-
?
additional information
?
-
-
the enzyme in the brain dopaminergix system is involved in the pathogenesis of doamine deficiency-dependent depressive states, and is activated in association with development of MPTP-induced depressive syndrome in the brain frontal cortex, overview
-
-
?
additional information
?
-
-
the enzyme is a serine protease, that digests small peptide-like hormones, neuroactive peptides, and various cellular factors, it is implicated in several biological processes and diseases, e.g. in some psychiatric disorders, most probably through interference in the inositol cycle, it is important in the metabolism of substance P, arginine vasopressin, thyroliberin, and gonadoliberin, enzyme regulation, overview
-
-
?
additional information
?
-
-
the enzyme is associated with cognitive functions and inositol 1,4,5-triphosphate signaling, and plays a role in modifying neuropeptide levels, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the phosphoinositide pathway, in formation and processing of amyloid beta-peptide, protein secretion, and in neuronal differentiation and maturation, overview, the enzyme is involved in several diseases, e.g. celiac disease, Alzheimer's diease, Parkinsons's disease, affective disorders, eating disorders, cancer, inflammation, hypertension, and neurodegenarative disorders, overview, enzyme inhibition can improve the retention time when administered before either the acquisition or the retential trial in scopolamine-induced amnesia, enzyme inhibition also positively affects neurodiseases, overview
-
-
?
additional information
?
-
-
the enzyme is involved with the inactivation of regulatory neuropeptides
-
-
?
additional information
?
-
-
the enzyme plays a role in inositol 1,4,5-triphosphate signaling and in the actions of antidepressants, POP inhibitors have antiamnesic and neuroprotective properties, overview
-
-
?
additional information
?
-
-
hydrolyzes proline-containing peptides shorter than 30 amino acids
-
-
?
additional information
?
-
-
is involved in thalamocortical and corticothalamic signal processing
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(S)-1-((S)-1-(4-phenylbutanoyl)-pyrrolidine-2-carbonyl)pyrrolidine-2-carbonitrile
-
KYP-2047, most potent inhibitor
1,2-oxazolidin-2-yl[(2S,3aS,7aS)-1-[[(1R,2R)-2-phenylcyclopropyl]carbonyl]octahydro-1H-indol-2-yl]methanone
-
-
1-[2-oxo-2-[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]ethyl]-3-phenylquinoxalin-2(1H)-one
-
-
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-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
-
-
3-[3-oxo-3-[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]propyl]-5,5-diphenylimidazolidine-2,4-dione
-
-
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
[(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
-
-
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
S 17092
-
selective enzyme inhibitor, pharmacodynamics and pharmacokinetics, overview
S-17092
-
i.e. (2S,3aS,7aS)-1-[[(R,R)-2-phenylcyclopropyl]carbonyl]-2-[(thiazolidin-3-yl)carbonyl] octahydro-1H-indole
additional information
-
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
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000029
(S)-1-((S)-1-(4-phenylbutanoyl)-pyrrolidine-2-carbonyl)pyrrolidine-2-carbonitrile
Rattus norvegicus
-
cell free assay, pH and temperature not specified in the publication
0.000002
1,2-oxazolidin-2-yl[(2S,3aS,7aS)-1-[[(1R,2R)-2-phenylcyclopropyl]carbonyl]octahydro-1H-indol-2-yl]methanone
Rattus norvegicus
-
rat cortex
0.00002
1-[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]octan-1-one
Rattus norvegicus
-
rat brain
0.00000088
1-[2-oxo-2-[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]ethyl]-3-phenylquinoxalin-2(1H)-one
Rattus norvegicus
-
rat brain
0.0000027
2,3-dihydro-1H-pyrrol-1-yl[(2S,3aS,7aS)-1-[[(1R,2R)-2-phenylcyclopropyl]carbonyl]octahydro-1H-indol-2-yl]methanone
Rattus norvegicus
-
rat cortex
0.0000024
2,5-dihydro-1H-pyrrol-1-yl[(2S,3aS,7aS)-1-[[(1R,2R)-2-phenylcyclopropyl]carbonyl]octahydro-1H-indol-2-yl]methanone
Rattus norvegicus
-
rat cortex
0.000003
2-[2-oxo-2-[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]ethyl]-1H-isoindole-1,3(2H)-dione
Rattus norvegicus
-
rat brain
0.00000081
2-[2-[(2S)-4,4-difluoro-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]-2-oxoethyl]-1H-isoindole-1,3(2H)-dione
Rattus norvegicus
-
rat brain
0.000041
3-[3-oxo-3-[(2S)-2-(pyrrolidin-1-ylcarbonyl)pyrrolidin-1-yl]propyl]-5,5-diphenylimidazolidine-2,4-dione
Rattus norvegicus
-
rat brain
0.00204
Boc-Asn-Phe-Pro-aldehyde
Rattus norvegicus
-
cell free assay, pH and temperature not specified in the publication
0.000733
Z-Pro-Pro-aldehyde-dimethylacetal
Rattus norvegicus
-
cell free assay, pH and temperature not specified in the publication
0.0000023
[(1R,2R)-2-phenylcyclopropyl][(2S,3aS,7aS)-2-(1H-pyrrol-1-ylcarbonyl)octahydro-1H-indol-1-yl]methanone
Rattus norvegicus
-
rat cortex
0.0000012
[(1R,2R)-2-phenylcyclopropyl][(2S,3aS,7aS)-2-(pyrrolidin-1-ylcarbonyl)octahydro-1H-indol-1-yl]methanone
Rattus norvegicus
-
rat cortex
0.000005
[(1R,2R)-2-phenylcyclopropyl][(3S)-3-(pyrrolidin-1-ylcarbonyl)-2-azabicyclo[2.2.2]oct-2-yl]methanone
Rattus norvegicus
-
rat cortex
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
-
-
distribution in brain tissues, immunohistochemic analysis, overview
-
distribution of POP immunoreactivity in the rat brain and its colocalizations with IP3R1 and SP markers shown
-
specific expression of POP in glutamatergic pyramidal neurons of the cerebral cortex, particularly in the primary motir and somatosensory cortices
-
in gamma-aminobutyratergic and cholinergic intermeurons of the thalamus and cortex, but not in the nigrostriatal dopaminergic neurons
additional information
-
no enzyme activity in intestinal brush-border membranes and pancreas
additional information
-
no enzyme in pancreatic/intestinal brush border membranes
additional information
-
the distribution of the enzsm in brain tissue correlates with the distribution of the IP3-receptor
additional information
-
tissue distribution, immunohistochemic analysis, overview, no localization with astrocytes
additional information
-
no expression of POP in granular layer, ventral tegmental area (midbrain), red nucleus (midbrain), superior colliculus (midbrain), inferior colliculus (midbrain)
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is located in the nucleus only early in the brain development
additional information
-
the enzyme is transferred to the cytosol already before parturition
additional information
-
cellular distribution, immunohistochemic analysis, overview
-
additional information
-
the highest levels in particulate fractions in the synaptosomal and the myelin fractions
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
important function in learning and memory processes, psychological disorders and neurodegenerative diseases
physiological function
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
-
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
-
prolyl oligopeptidase has a pro-angiogenic role via the release of acetyl-N-Ser-Asp-Lys-Pro from its precursor thymosin beta4
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PPCE_RAT
710
0
80742
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme has a two-domain structure whose unique seven-blade beta-propeller domain works with the catalytic domain, mechanism for peptide entry between the two domains, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
PO -/- mice with a targeted prolyl oligopeptidase null-mutation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after period of neuronal migration and differentiation decreasing expression, lowest levels in adulthood
enzymatic activity of POP is highest on embryonic day 18 while the protein amounts reach their peak at birth
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kobayashi, W.; Miyase, T.; Sano, M.; Umehara, K.; Warashina, T.; Noguchi, H.
Prolyl endopeptidase inhibitors from the roots of Lindera strychnifolia F. Vill
Biol. Pharm. Bull.
25
1049-1052
2002
Elizabethkingia meningoseptica, Rattus norvegicus
Irazusta, J.; Silveira, P.F.; Gil, J.; Varona, A.; Casis, L.
Effects of hydrosaline treatments on prolyl endopeptidase activity in rat tissues
Regul. Pept.
101
141-147
2001
Rattus norvegicus
Besedin, D.V.; Rudenskaya, G.N.
Proline-specific endopeptidases
Russ. J. Bioorg. Chem.
29
1-17
2003
Agaricus bisporus, Bos taurus, Cavia porcellus, Gallus gallus, Elizabethkingia meningoseptica, Oryctolagus cuniculus, Novosphingobium capsulatum, Ovis aries, Homo sapiens, Lyophyllum cinerascens, Mus musculus, Rattus norvegicus, Sus scrofa, Xanthomonas sp., Ascidia sp., Clupea pallasii, Lactifluus hygrophoroides, Russula lepida
-
Krupina, N.A.; Zolotov, N.N.; Bogdanova, N.G.; Orlova, I.N.; Khlebnikova, N.N.; Kryzhanovskii, G.N.
Activities of prolyl endopeptidase and dipeptidyl peptidase IV in brain structures of rats with dopamine deficiency-dependent MPTP-induced depressive syndrome
Bull. Exp. Biol. Med.
142
554-556
2006
Rattus norvegicus
Gass, J.; Khosla, C.
Prolyl endopeptidases
Cell. Mol. Life Sci.
64
345-355
2007
Elizabethkingia meningoseptica, Dictyostelium discoideum, Novosphingobium capsulatum, Homo sapiens, Mus musculus, Myxococcus xanthus, Pyrococcus furiosus, Rattus norvegicus, Sus scrofa
Brandt, I.; Scharpe, S.; Lambeir, A.M.
Suggested functions for prolyl oligopeptidase: a puzzling paradox
Clin. Chim. Acta
377
50-61
2007
Elizabethkingia meningoseptica, Homo sapiens, Mus musculus, Rattus norvegicus, Trypanosoma cruzi
Szeltner, Z.; Polgar, L.
Structure, function and biological relevance of prolyl oligopeptidase
Curr. Protein Pept. Sci.
9
96-107
2008
Elizabethkingia meningoseptica, Dictyostelium discoideum, Novosphingobium capsulatum, Homo sapiens, Platyrrhini, Mus musculus, Myxococcus xanthus, Pyrococcus furiosus, Rattus norvegicus, Sus scrofa
Myoehaenen, T.T.; Venaelaeinen, J.I.; Garcia-Horsman, J.A.; Piltonen, M.; Maennistoe, P.T.
Cellular and subcellular distribution of rat brain prolyl oligopeptidase and its association with specific neuronal neurotransmitters
J. Comp. Neurol.
507
1694-1708
2008
Rattus norvegicus
Myoehaenen, T.T.; Venaelaeinen, J.I.; Tupala, E.; Garcia-Horsman, J.A.; Miettinen, R.; Maennistoe, P.T.
Distribution of immunoreactive prolyl oligopeptidase in human and rat brain
Neurochem. Res.
32
1365-1374
2007
Homo sapiens, Rattus norvegicus
Garcia-Horsman, J.A.; Maennistoe, P.T.; Venaelaeinen, J.I.
On the role of prolyl oligopeptidase in health and disease
Neuropeptides
41
1-24
2007
Dictyostelium discoideum, Novosphingobium capsulatum, Flavobacterium sp., Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa (P23687)
Di Daniel, E.; Glover, C.P.; Grot, E.; Chan, M.K.; Sanderson, T.H.; White, J.H.; Ellis, C.L.; Gallagher, K.T.; Uney, J.; Thomas, J.; Maycox, P.R.; Mudge, A.W.
Prolyl oligopeptidase binds to GAP-43 and functions without its peptidase activity
Mol. Cell. Neurosci.
41
373-382
2009
Rattus norvegicus (O70196)
Myoehaenen, T.T.; Kaeaeriaeinen, T.M.; Jalkanen, A.J.; Piltonen, M.; Maennistoe, P.T.
Localization of prolyl oligopeptidase in the thalamic and cortical projection neurons: a retrograde neurotracing study in the rat brain
Neurosci. Lett.
450
201-205
2009
Rattus norvegicus
Myoehaenen, T.T.; Venaelaeinen, J.I.; Garcia-Horsman, J.A.; Maennistoe, P.T.
Spatial association of prolyl oligopeptidase, inositol 1,4,5-triphosphate type 1 receptor, substance P and its neurokinin-1 receptor in the rat brain: an immunohistochemical colocalization study
Neuroscience
153
1177-1189
2008
Rattus norvegicus
Tenorio-Laranga, J.; Valero, M.L.; Maennistoe, P.T.; Sanchez del Pino, M.; Garcia-Horsman, J.A.
Combination of snap freezing, differential pH two-dimensional reverse-phase high-performance liquid chromatography, and iTRAQ technology for the peptidomic analysis of the effect of prolyl oligopeptidase inhibition in the rat brain
Anal. Biochem.
393
80-87
2009
Rattus norvegicus
Peltonen, I.; Jalkanen, A.J.; Sinervae, V.; Puttonen, K.A.; Maennistoe, P.T.
Different effects of scopolamine and inhibition of prolyl oligopeptidase on mnemonic and motility functions of young and 8- to 9-month-old rats in the radial-arm maze
Basic Clin. Pharmacol. Toxicol.
106
280-287
2010
Rattus norvegicus
Khlebnikova, N.N.; Krupina, N.A.; Bogdanova, N.G.; Zolotov, N.N.; Kryzhanovskii, G.N.
Effects of prolylendopeptidase inhibitor benzyloxycarbonyl-methionyl-2(S)-cyanopyrrolidine on experimental depressive syndrome development in rats
Bull. Exp. Biol. Med.
147
26-30
2009
Rattus norvegicus
Khlebnikova, N.N.; Krupina, N.A.; Orlova, I.N.; Bogdanova, N.G.; Zolotov, N.N.; Kryzhanovskii, G.N.
Effect of a prolyl endopeptidase inhibitor benzyloxycarbonyl-alanyl-proline on the development of experimental depressive syndrome in rats
Bull. Exp. Biol. Med.
147
291-295
2009
Rattus norvegicus
Agirregoitia, N.; Bizet, P.; Agirregoitia, E.; Boutelet, I.; Peralta, L.; Vaudry, H.; Jegou, S.
Prolyl endopeptidase mRNA expression in the central nervous system during rat development
J. Chem. Neuroanat.
40
53-62
2010
Rattus norvegicus (O70196)
Lawandi, J.; Gerber-Lemaire, S.; Juillerat-Jeanneret, L.; Moitessier, N.
Inhibitors of prolyl oligopeptidases for the therapy of human diseases: Defining diseases and inhibitors
J. Med. Chem.
53
3423-3438
2010
Bos taurus, Canis lupus familiaris, Elizabethkingia meningoseptica, Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa (P23687)
Peltonen, I.; Maennistoe, P.T.
Effects of diverse psychopharmacological substances on the activity of brain prolyl oligopeptidase
Basic Clin. Pharmacol. Toxicol.
108
46-54
2011
Rattus norvegicus
Myoehaenen, T.T.; Tenorio-Laranga, J.; Jokinen, B.; Vazquez-Sanchez, R.; Moreno-Baylach, M.J.; Garcia-Horsman, J.A.; Maennistoe, P.T.
Prolyl oligopeptidase induces angiogenesis both in vitro and in vivo in a novel regulatory manner
Br. J. Pharmacol.
163
1666-1678
2011
Homo sapiens, Rattus norvegicus
Hannula, M.J.; Maennistoe, P.T.; Myoehaenen, T.T.
Sequential expression, activity and nuclear localization of prolyl oligopeptidase protein in the developing rat brain
Dev. Neurosci.
33
38-47
2011
Rattus norvegicus
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