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Information on EC 3.4.16.2 - lysosomal Pro-Xaa carboxypeptidase and Organism(s) Homo sapiens
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3.4.16.2 lysosomal Pro-Xaa carboxypeptidaseSpecify your search results
Word Map
- 3.4.16.2
- aminopeptidase
- potato
- pancreatic
-
fibrinolysis
- cathepsins
- bradykinin
-
b-like
-
angiotensin-converting
-
mast
- thrombin
- clot
-
exopeptidase
- neuropeptides
-
edman
- chymotrypsin
- plasminogen
-
dipeptidyl
- ace2
- tafia
- enkephalin
- kinin
-
thrombin-activatable
- zymogen
- endopeptidases
- fibrin
-
convertase
-
kininase
-
activatable
- plasmin
-
prohormone
- chymase
- anaphylatoxins
-
trypsin-like
- thrombomodulin
- tryptase
-
endoproteolytic
-
detyrosinated
- captopril
-
i-converting
-
galactosialidosis
-
antifibrinolytic
- leech
-
polyglutamylation
-
3.4.15.1
- bestatin
- phosphoramidon
- c3a
- enkephalinase
- kallidin
-
transpeptidation
- analysis
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
carboxypeptidase, plasma carboxypeptidase, prolyl carboxypeptidase, lysosomal carboxypeptidase, carboxypeptidase a6, angiotensinase c, lysosomal pro-x carboxypeptidase, matrix pk activator, serine protease prolylcarboxypeptidase, lysosomal pro-xaa carboxypeptidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminoacylproline carboxypeptidase
-
-
-
-
angiotensinase C
-
-
-
-
Carboxypeptidase P
-
-
-
-
carboxypeptidase, aminoacylproline
-
-
-
-
carboxypeptidase, peptidylprolylamino acid
-
-
-
-
lysosomal carboxypeptidase
-
-
-
-
lysosomal carboxypeptidase C
-
-
-
-
PCP
-
-
-
-
PRCP
proline carboxypeptidase
-
-
-
-
proline-specific carboxypeptidase P
-
-
-
-
prolyl carboxypeptidase
-
-
-
-
prolylcarboxypeptidase
PRCP
-
-
-
-
PRCP
-
-
prolylcarboxypeptidase
-
-
-
-
prolylcarboxypeptidase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY
9075-64-3
-
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
3-(2-furyl)acryloyl-peptide + H2O
?
-
substrate used in the carboxypeptidase assay
-
-
?
angiotensin III + H2O
angiotensin 2-7 + phenylalanine
-
mutant DELTA317-496 is able to carry out this reaction
-
-
?
N-benzyloxycarbonyl-L-Pro-L-Ala + H2O
N-benzyloxycarbonyl-L-Pro + L-Ala
-
-
-
-
?
N-benzyloxycarbonyl-Pro-Leu + H2O
N-benzyloxycarbonyl-Pro + Leu
-
12% of the activity with angiotensin III
-
-
?
N-benzyloxycarbonyl-Pro-Ser + H2O
N-benzyloxycarbonyl-Pro + Ser
-
7% of the activity with angiotensin III
-
-
?
YPRPIHPA + H2O
?
-
using a peptidomic approach a single peptide YPRPIHPA is identified as a novel substrate for PRCP in human cerebrospinal fluid. The peptide YPRPIHPA is from the extracellular portion of human endothelin B receptor like protein 2
-
-
?
angiotensin II + H2O
?
-
about 35% of the activity with angiotensin III
-
-
?
N-benzyloxycarbonyl-Pro-Ala + H2O
N-benzyloxycarbonyl-Pro + Ala
-
33% of the activity with angiotensin III
-
-
?
N-benzyloxycarbonyl-Pro-Phe + H2O
N-benzyloxycarbonyl-Pro + Phe
-
8% of the activity with angiotensin III
-
?
N-benzyloxycarbonyl-Pro-Phe + H2O
N-benzyloxycarbonyl-Pro + Phe
-
8% of the activity with angiotensin III
-
-
?
N-benzyloxycarbonyl-Pro-Val + H2O
N-benzyloxycarbonyl-Pro + Val
-
28% of the activity with angiotensin III
-
-
?
additional information
?
-
-
overexpression of prolylcarboxypeptidase enhances plasma prekallikrein activation on Chinese hamster ovary cells
-
-
?
additional information
?
-
-
the enzyme is a plasma prekallikrein activator
-
-
?
prekallikrein + H2O
additional information
-
-
-
production of a 51000 Da heavy chain and 2 faint light chains of 39000 Da and 36000 Da
?
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
YPRPIHPA + H2O
?
-
using a peptidomic approach a single peptide YPRPIHPA is identified as a novel substrate for PRCP in human cerebrospinal fluid. The peptide YPRPIHPA is from the extracellular portion of human endothelin B receptor like protein 2
-
-
?
additional information
?
-
-
overexpression of prolylcarboxypeptidase enhances plasma prekallikrein activation on Chinese hamster ovary cells
-
-
?
additional information
?
-
-
the enzyme is a plasma prekallikrein activator
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3R,4R)-4-[3-(4-chlorophenyl)-1H-pyrazol-5-yl]-1-(2,2-dimethylpropyl)-3-(4-fluorophenyl)piperidine
-
compound shows improved oral bioavailabilities
2-[4-[3-(4-fluorophenyl)-1-methyl-1H-pyrazol-5-yl]-1-(2-phenylethyl)piperidin-4-yl]pyridine
-
most potent compound in the series
benzyloxycarbonyl-Pro-prolinal
-
IC50: 0.5 mM, inhibits hydrolysis of H-Gly-Pro-4-nitroanilide
[(3S,4R)-1-tert-butyl-4-(2,4-difluorophenyl)pyrrolidin-3-yl](4-[(1Z)-1-[(2,5-dichlorophenyl)amino]-3-iminobut-1-en-1-yl]piperidin-1-yl)methanone
-
-
[(3S,4R)-1-tert-butyl-4-(2,4-difluorophenyl)pyrrolidin-3-yl](4-[(1Z)-1-[(3-chloro-4-fluorophenyl)amino]-3-iminoprop-1-en-1-yl]piperidin-1-yl)methanone
-
-
[4-[1-(3-chloro-4-fluorophenyl)-1H-pyrazol-5-yl]piperidin-1-yl][(1R,2R,4S)-2-(2,4-difluorophenyl)-4-(dimethylamino)-4-methylcyclopentyl]methanone
-
-
corn trypsin inhibitor
-
binds to prekallikrein to prevent activation, but does not directly inhibit the active site of either enzyme
-
additional information
-
no inhibition by 1 mM EDTA, bradykinin 1-5 or angiotensin 1-7
-
additional information
-
no inhibition by 1 mM EDTA, bradykinin1-5, or angiotensin 1-7
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
in cells, treated with 30 nM dexamethasone plus 1 nM DAMGO ([D-Ala2, N-Me-Phe4, Gly5-ol]-Enkephalin), the prolyl-carboxypeptidase gene is up-regulated
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000066
(3R,4R)-4-[3-(4-chlorophenyl)-1H-pyrazol-5-yl]-1-(2,2-dimethylpropyl)-3-(4-fluorophenyl)piperidine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000033
2-[4-[3-(4-fluorophenyl)-1-methyl-1H-pyrazol-5-yl]-1-(2-phenylethyl)piperidin-4-yl]pyridine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.5
benzyloxycarbonyl-Pro-prolinal
Homo sapiens
-
IC50: 0.5 mM, inhibits hydrolysis of H-Gly-Pro-4-nitroanilide
0.1
N-(9-fluorenyl)methoxycarbonyl-aminoacylpyrrolidine-2-nitrile
Homo sapiens
-
IC50: 0.1 mM
0.0000003
[(3S,4R)-1-tert-butyl-4-(2,4-difluorophenyl)pyrrolidin-3-yl](4-[(1Z)-1-[(2,5-dichlorophenyl)amino]-3-iminobut-1-en-1-yl]piperidin-1-yl)methanone
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000002
[(3S,4R)-1-tert-butyl-4-(2,4-difluorophenyl)pyrrolidin-3-yl](4-[(1Z)-1-[(3-chloro-4-fluorophenyl)amino]-3-iminoprop-1-en-1-yl]piperidin-1-yl)methanone
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0000003
[4-[1-(3-chloro-4-fluorophenyl)-1H-pyrazol-5-yl]piperidin-1-yl][(1R,2R,4S)-2-(2,4-difluorophenyl)-4-(dimethylamino)-4-methylcyclopentyl]methanone
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 5.5
4.5 - 5.5
-
with N-benzyloxycarbonyl-Pro-Phe, angiotensin II or angiotensin III as substrate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 7
4.5 - 7
-
pH 4.5-5.0: optimal pH with N-benzyloxycarbonyl-Pro-Phe, angiotensin II or angiotensin III as substrate, pH 7: 9% of maximal activity with N-benzyloxycarbonyl-Pro-Phe, 20% of maximal activity with angiotensin II, 50% of maximal activity with angiotensin III
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the 37-kDa active form of the protein is secreted into the extracellular matrix
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
upregulation of PRCP in lipopolysaccharide treated endothelium promotes inflammation
physiological function
-
prolyl carboxypeptidase and the related family member prolyl endopeptidase are essential for proliferation and survival of pancreatic cancer cells. Depletion/inhibition of prolyl carboxypeptidase and prolyl endopeptidase induces serine phosphorylation and degradation of insulin receptor substrate IRS-1, leading to inactivation of the cellular PI3K and AKT. Depletion/inhibition of prolyl carboxypeptidase /prolyl endopeptidase destabilized IRS-1 in the cells treated with rapamycin, blocking the feedback activation PI3K/AKT. Inhibition of prolyl carboxypeptidase /prolyl endopeptidase enhances rapamycin-induced cytotoxicity
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). PCP_HUMAN
496
1
55800
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
prolylcarboxypeptidase has six potential N-glycosylation sites, suggesting that it undergoes post-translational modifications
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization of glycosylated human PrCP from stably transformed CHO cells is described. Purified PrCP yields crystals belonging to space group R32, with unit-cell parameters a = b = 181.14, c = 240.13 A, that diffract to better than 2.8 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA317-496
-
an N-terminal truncated form, lacking 179 N-terminal residues of PRCP is constructed. The circular dichroism spectrum of the truncated mutant illustrates that it is structured with significant helical content as indicated by local minima at 220 and 208 nm. The main products of angiotensin III metabolized by the truncated mutant is angiotensin 2-7 plus phenylalanine as determined by LC-MS. Angiotensin I blockes the metabolism of angiotensin III by the truncated mutant. Km (mM) (Ala-Pro-4-nitroanilide) lower compared to wild-type
E112D
E112D
-
prolylcarboxypeptidase E112D (rs22988668) D allele along and jointly with chronic hypertension are associated with a significant increased risk of preeclampsia
E112D
-
E112D polymorphism in the PRCP gene is associated with blood pressure response to benazepril in Chinese hypertensive patients
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Chineses hamster ovary cells. CHO cells are transfected with full-length prolylcarboxypeptidase under the control of a cytomegalovirus promoter. CHO recombinant prolylcarboxypeptidase is expressed as a fusion protein with COOH-terminal enhanced green fluorescence protein. Overexpression in the external membrane
-
PrCP is cloned with an N-terminal FLAG tag and a C-terminal heptahistidine tag under the trypsin II signal sequence in pcDNA5/FRT and expressed in stably transfected CHO cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
PRCP is critical to the maintenance of HUVEC cells, and its upregulation contributes to the risk of developing inflammation
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
E112D could be a highly sensitive and specific early predictor of preeclampsia among woman with chronic hypertension
medicine
-
the results could provide new therapeutic opportunity for the treatment of infection
medicine
-
the validity of prolylcarboxypeptidase as a site specific therapeutic that could mitigate inflammatory injury is discussed
medicine
-
E112D polymorphism in the PRCP gene may be a useful genetic marker to predict the antihypertensive effect of short-term benazepril treatment in hypertensive patients of Anhui Province, China
medicine
-
analysis of prolyl carboxypeptidase activity in serum of 50 stroke patients at admission, and at 24 h, 72 h and 7 days after stroke onset. The decrease in prolyl carboxypeptidase levels in the first 24 h after stroke onset is associated with stroke severity and an unfavourable short-term stroke outcome. High National Institutes of Health Stroke scale scores and infarct volumes at admission are related with a more pronounced decrease of prolyl carboxypeptidase in the first 24 h after stroke
medicine
-
prolyl carboxypeptidase and prolyl endopeptidase regulate insulin receptor substrate IRS-1 stability and PI3K/AKT activation in pancreatic cancer
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tan, F.; Morris, P.W.; Skidgel, R.A.; Erdös, E.G.
Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C). Similarity to both serine carboxypeptidase and prolylendopeptidase families [published erratum appears in J Biol Chem 1993 Dec 5;268(34):26032
J. Biol. Chem.
268
16631-16638
1993
Homo sapiens
Odya, C.E.; Erdös, E.G.
Human prolylcarboxypeptidase
Methods Enzymol.
80
460-466
1981
Homo sapiens
Skidgel, R.A.; Wickstrom, E.; Kumamoto, K.; Erdös, E.G.
Rapid radioassay for prolylcarboxypeptidase (angiotensinase C)
Anal. Biochem.
118
113-119
1981
Homo sapiens
Odya, C.E.; Marinkovic, D.V.; Hammon, K.J.; Stewart, T.A.; Erdös, E.G.
Purification and properties of prolylcarboxypeptidase (angiotensinase C) from human kidney
J. Biol. Chem.
253
5927-5931
1978
Homo sapiens
Yang, H.Y.T.; Erdös, E.G.; Chiang, T.S.
New enzymatic route for the inactivation of angiotensin
Nature
218
1224-1226
1968
Homo sapiens, Sus scrofa
Jackman, H.L.; Tan, F.; Schraufnagel, D.; Dragovic, T.; Dezsö, B.; Becker, R.P.; Erdös, E.G.
Plasma membrane-bound and lysosomal peptidases in human alveolar macrophages
Am. J. Respir. Cell Mol. Biol.
13
196-204
1995
Homo sapiens
Gacko, M.; Worowska, A.; Glowinski, S.
Activity of lysosomal carboxypeptidase in aneurysmal aortic wall
Bull. Pol. Acad. Sci. Biol. Sci.
46
107-112
1998
Homo sapiens
-
Shariat-Madar, Z.; Mahdi, F.; Schmaier, A.H.
Recombinant prolylcarboxypeptidase activates plasma prekallikrein
Blood
15
4554-4561
2004
Homo sapiens
Moreira, C.R.; Schmaier, A.H.; Mahdi, F.; da Motta, G.; Nader, H.B.; Shariat-Madar, Z.
Identification of prolylcarboxypeptidase as the cell matrix-associated prekallikrein activator
FEBS Lett.
523
167-170
2002
Homo sapiens
Shariat-Madar, Z.; Mahdi, F.; Schmaier, A.H.
Identification and characterization of prolylcarboxypeptidase as an endothelial cell prekallikrein activator
J. Biol. Chem.
277
17962-17969
2002
Homo sapiens
Shariat-Madar, Z.; Rahimy, E.; Mahdi, F.; Schmaier, A.H.
Overexpression of prolylcarboxypeptidase enhances plasma prekallikrein activation on Chinese hamster ovary cells
Am. J. Physiol.
289
H2697-H2703
2005
Homo sapiens
Shariat-Madar, Z.; Mahdi, F.; Schmaier, A.H.
Recombinant prolylcarboxypeptidase activates plasma prekallikrein
Blood
103
4554-4561
2004
Homo sapiens
Wang, L.; Feng, Y.; Zhang, Y.; Zhou, H.; Jiang, S.; Niu, T.; Wei, L.J.; Xu, X.; Xu, X.; Wang, X.
Prolylcarboxypeptidase gene, chronic hypertension, and risk of preeclampsia
Am. J. Obstet. Gynecol.
195
162-171
2006
Homo sapiens
Perkins, R.; Ngo, M.D.; Mahdi, F.; Shariat-Madar, Z.
Identification of lipopolysaccharide binding site on high molecular weight kininogen
Biochem. Biophys. Res. Commun.
366
938-943
2008
Homo sapiens
Ward, G.R.; Franklin, S.O.; Gerald, T.M.; Dempsey, K.T.; Clodfelter, D.E.; Krissinger, D.J.; Patel, K.M.; Vrana, K.E.; Howlett, A.C.
Glucocorticoids plus opioids up-regulate genes that influence neuronal function
Cell. Mol. Neurobiol.
27
651-660
2007
Homo sapiens
Mallela, J.; Yang, J.; Shariat-Madar, Z.
Prolylcarboxypeptidase: A cardioprotective enzyme
Int. J. Biochem. Cell Biol.
41
477-481
2009
Homo sapiens
Lyons, P.J.; Callaway, M.B.; Fricker, L.D.
Characterization of carboxypeptidase a6, an extracellular matrix peptidase
J. Biol. Chem.
283
7054-7063
2008
Homo sapiens
Mallela, J.; Perkins, R.; Yang, J.; Pedigo, S.; Rimoldi, J.M.; Shariat-Madar, Z.
The functional importance of the N-terminal region of human prolylcarboxypeptidase
Biochem. Biophys. Res. Commun.
374
635-640
2008
Homo sapiens
Abeywickrema, P.D.; Patel, S.B.; Byrne, N.J.; Diehl, R.E.; Hall, D.L.; Ford, R.E.; Rickert, K.W.; Reid, J.C.; Shipman, J.M.; Geissler, W.M.; Pryor, K.D.; SinhaRoy, R.; Soisson, S.M.; Lumb, K.J.; Sharma, S.
Expression, purification and crystallization of human prolylcarboxypeptidase
Acta Crystallogr. Sect. F
66
702-705
2010
Homo sapiens (P42785)
Zhang, Y.; Hong, X.M.; Xing, H.X.; Li, J.P.; Huo, Y.; Xu, X.P.
E112D polymorphism in the prolylcarboxypeptidase gene is associated with blood pressure response to benazepril in Chinese hypertensive patients
Chin. Med. Sci.
122
2461-2465
2009
Homo sapiens
Ngo, M.L.; Mahdi, F.; Kolte, D.; Shariat-Madar, Z.
Upregulation of prolylcarboxypeptidase (PRCP) in lipopolysaccharide (LPS) treated endothelium promotes inflammation
J. Inflamm.
6
1-9
2009
Homo sapiens
Zhao, X.; Southwick, K.; Cardasis, H.L.; Du, Y.; Lassman, M.E.; Xie, D.; El-Sherbeini, M.; Geissler, W.M.; Pryor, K.D.; Verras, A.; Garcia-Calvo, M.; Shen, D.M.; Yates, N.A.; Pinto, S.; Hendrickon, R.C.
Peptidomic profiling of human cerebrospinal fluid identifies YPRPIHPA as a novel substrate for prolylcarboxypeptidase
Proteomics
10
2882-2886
2010
Homo sapiens
Graham, T.H.; Liu, W.; Verras, A.; Sebhat, I.K.; Xiong, Y.; Bleasby, K.; Bhatt, U.R.; Chen, Q.; Garcia-Calvo, M.; Geissler, W.M.; Gorski, J.N.; He, H.; Lassman, M.E.; Lisnock, J.; Li, X.; Shen, Z.; Tong, X.; Tung, E.C.; Wiltsie, J.; Xiao, J.; Xie, D.; Xu, S.; Hale, J.J.; Pinto, S.; Shen, D.M.
A new class of prolylcarboxypeptidase inhibitors, part 1: discovery and evaluation
Bioorg. Med. Chem. Lett.
22
2811-2817
2012
Homo sapiens, Mus musculus
Graham, T.H.; Liu, W.; Verras, A.; Reibarkh, M.; Bleasby, K.; Bhatt, U.R.; Chen, Q.; Garcia-Calvo, M.; Geissler, W.M.; Gorski, J.N.; He, H.; Lassman, M.E.; Lisnock, J.; Li, X.; Shen, Z.; Tong, X.; Tung, E.C.; Wiltsie, J.; Xie, D.; Xu, S.; Xiao, J.; Hale, J.J.; Pinto, S.; Shen, D.M.
A new class of prolylcarboxypeptidase inhibitors, part 2: the aminocyclopentanes
Bioorg. Med. Chem. Lett.
22
2818-2822
2012
Homo sapiens, Mus musculus
Graham, T.H.; Shu, M.; Verras, A.; Chen, Q.; Garcia-Calvo, M.; Li, X.; Lisnock, J.; Tong, X.; Tung, E.C.; Wiltsie, J.; Hale, J.J.; Pinto, S.; Shen, D.M.
Pyrazoles as non-classical bioisosteres in prolylcarboxypeptidase (PrCP) inhibitors
Bioorg. Med. Chem. Lett.
24
1657-1660
2014
Homo sapiens, Mus musculus
Duan, L.; Ying, G.; Danzer, B.; Perez, R.E.; Shariat-Madar, Z.; Levenson, V.V.; Maki, C.G.
The prolyl peptidases PRCP/PREP regulate IRS-1 stability critical for rapamycin-induced feedback activation of PI3K and AKT
J. Biol. Chem.
289
21694-21705
2014
Homo sapiens
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