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Information on EC 3.4.16.2 - lysosomal Pro-Xaa carboxypeptidase and Organism(s) Homo sapiens and UniProt Accession P42785

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Homo sapiens
UNIPROT: P42785 not found.
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The taxonomic range for the selected organisms is: Homo sapiens
Reaction Schemes
Cleavage of a -Pro-/-Xaa bond to release a C-terminal amino acid
Synonyms
aminoacylproline carboxypeptidase, angiotensinase C, carboxypeptidase, carboxypeptidase A6, Carboxypeptidase P, Carboxypeptidase R, carboxypeptidase, aminoacylproline, carboxypeptidase, peptidylprolylamino acid, CPA6, CPP, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminoacylproline carboxypeptidase
-
-
-
-
angiotensinase C
-
-
-
-
carboxypeptidase A6
247
-
Carboxypeptidase P
-
-
-
-
carboxypeptidase, aminoacylproline
-
-
-
-
carboxypeptidase, peptidylprolylamino acid
-
-
-
-
CPA6
247
-
endothelial cell prekallikrein activator
247
-
HUVEC PK activator
247
-
lysosomal carboxypeptidase
-
-
-
-
lysosomal carboxypeptidase C
-
-
-
-
matrix PK activator
247
-
PCP
-
-
-
-
PKA
247
-
proline carboxypeptidase
-
-
-
-
proline-specific carboxypeptidase P
-
-
-
-
prolyl carboxypeptidase
-
-
-
-
prolyl-carboxypeptidase
247
-
prolylcarboxypeptidase
serine protease prolylcarboxypeptidase
247
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9075-64-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
7-methoxycoumarin-4-acetyl-Pro-Pro-Lys + H2O
?
show the reaction diagram
-
-
-
?
3-(2-furyl)acryloyl-peptide + H2O
?
show the reaction diagram
-
substrate used in the carboxypeptidase assay
-
-
?
Ala-Pro-4-nitroanilide + H2O
Ala-Pro + 4-nitroaniline
show the reaction diagram
Angiotensin II + H2O
?
show the reaction diagram
angiotensin III + H2O
?
show the reaction diagram
-
-
-
-
?
angiotensin III + H2O
angiotensin 2-7 + phenylalanine
show the reaction diagram
-
mutant DELTA317-496 is able to carry out this reaction
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-Pro-Ala + H2O
N-benzyloxycarbonyl-Pro + Ala
show the reaction diagram
N-benzyloxycarbonyl-Pro-Leu + H2O
N-benzyloxycarbonyl-Pro + Leu
show the reaction diagram
-
12% of the activity with angiotensin III
-
-
?
N-benzyloxycarbonyl-Pro-Phe + H2O
N-benzyloxycarbonyl-Pro + Phe
show the reaction diagram
N-benzyloxycarbonyl-Pro-Ser + H2O
N-benzyloxycarbonyl-Pro + Ser
show the reaction diagram
-
7% of the activity with angiotensin III
-
-
?
N-benzyloxycarbonyl-Pro-Val + H2O
N-benzyloxycarbonyl-Pro + Val
show the reaction diagram
prekallikrein + H2O
?
show the reaction diagram
-
-
-
?
saralasin + H2O
?
show the reaction diagram
-
-
-
-
?
YPRPIHPA + H2O
?
show the reaction diagram
-
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
-
-
?
[des-Arg9]bradykinin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
YPRPIHPA + H2O
?
show the reaction diagram
-
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
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CaCl2
-
optimal activity at 0.01 mM
MgCl2
-
optimal activity at 1 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
angiotensin I
-
inhibits the mutant DELTA317-496 in a dose-dependent manner
angiotensin II
Angiotensin III
-
inhibits the mutant DELTA317-496 in a dose-dependent manner
antipain
benzyloxycarbonyl-Pro-Pro-aldehyde dimethyl acetal
-
IC50: 0.001 mM
-
benzyloxycarbonyl-Pro-Pro-aldehyde-dimethyl acetate
-
-
-
benzyloxycarbonyl-Pro-prolinal
-
IC50: 0.5 mM, inhibits hydrolysis of H-Gly-Pro-4-nitroanilide
Benzylsuccinic acid
-
-
bradykinin
bradykinin anti-PRCP
-
-
-
corn trypsin inhibitor
-
diisopropyl fluorophosphate
diisopropyl fluorophosphonate
ebelactone B
-
noncompetitive
HgCl2
-
IC50: 0.5 mM
leupeptin
N-(9-fluorenyl)methoxycarbonyl-Ala-Pyr-CN
-
IC50: 50 nM
N-(9-fluorenyl)methoxycarbonyl-aminoacylpyrrolidine-2-nitrile
-
IC50: 0.1 mM
N-benzyloxycarbonyl-Pro-prolinal
-
-
NEM
-
3 mM, 30% inhibition
p-chloromercuriphenylsulfonic acid
-
1 mM, 15% inhibition
PCMB
-
1 mM, 15% inhibition
pepstatin
phenylmethyl sulfonyl fluoride
-
3 mM
phenylmethylsulfonyl fluoride
potato carboxypeptidase inhibitor
-
-
-
protease inhibitors of the blood plasma
-
-
-
Z-Pro-prolinal
-
-
[(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
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
IMAGE
1.5 - 3.1
Ala-Pro-4-nitroanilide
1
angiotensin II
-
-
2
Angiotensin III
-
-
4
Gly-Pro-4-nitroanilide
-
pH 5.5, 37C
4.7
N-benzyloxycarbonyl-L-Pro-L-Ala
-
-
0.77
N-benzyloxycarbonyl-Pro-Phe
-
-
0.0000067 - 0.000017
prekallikrein
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
210
YPRPIHPA
-
determined by an in vitro assay using human recombinant PRCP
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
1
angiotensin I
Homo sapiens
-
-
0.002 - 3
angiotensin II
0.002 - 0.05
antipain
0.001
benzyloxycarbonyl-Pro-Pro-aldehyde dimethyl acetal
Homo sapiens
-
IC50: 0.001 mM
-
0.5
benzyloxycarbonyl-Pro-prolinal
Homo sapiens
-
IC50: 0.5 mM, inhibits hydrolysis of H-Gly-Pro-4-nitroanilide
0.007
Benzylsuccinic acid
Homo sapiens
-
-
0.1 - 3
bradykinin
0.00004 - 0.0001
corn trypsin inhibitor
-
0.00005
diisopropyl fluorophosphonate
Homo sapiens
-
IC50: 50 nM
0.5
HgCl2
Homo sapiens
-
IC50: 0.5 mM
0.8
leupeptin
Homo sapiens
-
IC50: 0.8 mM, inhibits hydrolysis of Gly-Pro-4-nitroanilide
0.00005
N-(9-fluorenyl)methoxycarbonyl-Ala-Pyr-CN
Homo sapiens
-
IC50: 50 nM
0.1
N-(9-fluorenyl)methoxycarbonyl-aminoacylpyrrolidine-2-nitrile
Homo sapiens
-
IC50: 0.1 mM
0.6
phenylmethylsulfonyl fluoride
Homo sapiens
-
IC50: 0.6 mM
0.00005
potato carboxypeptidase inhibitor
Homo sapiens
-
-
-
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 hide
LITERATURE
0.51
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
assay at
4.5 - 5.5
5.8
-
assay at
7.5
-
carboxypeptidase assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7
6.8 - 7.4
-
more than 75% of maximal activity at pH 6.8 and pH 7.4
7 - 9
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
assay at room temperature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.9
-
predicted
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
aortic aneurysm and normal aorta
Manually annotated by BRENDA team
-
pancreatic cancer cell line
Manually annotated by BRENDA team
-
embryonic tissue
Manually annotated by BRENDA team
-
used for transfection
Manually annotated by BRENDA team
-
RNA is extracted from leukocytes
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
pancreatic cancer cell line
Manually annotated by BRENDA team
-
prolylcarboxypeptidase transcript levels are compared
Manually annotated by BRENDA team
-
pancreatic cancer cell line
Manually annotated by BRENDA team
-
foreskin fibroblast
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the 37-kDa active form of the protein is secreted into the extracellular matrix
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
PCP_HUMAN
496
1
55800
Swiss-Prot
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
-
active form, determined by SDS-PAGE and Western blot analysis
40000
-
mutant DELTA317-496
45000
-
x * 45000 + x * 66500, SDS-PAGE in presence of 2-mercaptoethanol
50000
-
pro-CPA6, determined by SDS-PAGE and Western blot analysis
51043
-
x * 51043, calculation from nucleotide sequence
52000
-
predicted from cDNA
55800
-
-
58000
-
x * 58000, SDS-PAGE
66500
-
x * 45000 + x * 66500, SDS-PAGE in presence of 2-mercaptoethanol
110000
-
gel filtration
115000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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 hide
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
half-life: 240 min
60
-
30 min, 20% loss of activity
70
-
15 min, 90% loss of activity
95
-
3 min, complete loss of activity
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
using Ni-affinity chromatography
recombinant
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
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
a cDNA fragment encoding human pro-CPA6 is subcloned into the pcDNA3.1 vector; expressed in AT-20 cells
-
cDNA cloned in pMT/BIP/V5-HIS-C, transfected into Schneider insect cells
-
cloned in pMT/BIP/V5-HIS-C, transfected into Scheider insect cells
-
expressed in Schneider insect cells
-
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
-
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 hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tan, F.; Morris, P.W.; Skidgel, R.A.; Erds, 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
Manually annotated by BRENDA team
Odya, C.E.; Erds, E.G.
Human prolylcarboxypeptidase
Methods Enzymol.
80
460-466
1981
Homo sapiens
Manually annotated by BRENDA team
Skidgel, R.A.; Wickstrom, E.; Kumamoto, K.; Erds, E.G.
Rapid radioassay for prolylcarboxypeptidase (angiotensinase C)
Anal. Biochem.
118
113-119
1981
Homo sapiens
Manually annotated by BRENDA team
Odya, C.E.; Marinkovic, D.V.; Hammon, K.J.; Stewart, T.A.; Erds, E.G.
Purification and properties of prolylcarboxypeptidase (angiotensinase C) from human kidney
J. Biol. Chem.
253
5927-5931
1978
Homo sapiens
Manually annotated by BRENDA team
Yang, H.Y.T.; Erds, E.G.; Chiang, T.S.
New enzymatic route for the inactivation of angiotensin
Nature
218
1224-1226
1968
Homo sapiens, Sus scrofa
Manually annotated by BRENDA team
Jackman, H.L.; Tan, F.; Schraufnagel, D.; Dragovic, T.; Dezs, B.; Becker, R.P.; Erds, E.G.
Plasma membrane-bound and lysosomal peptidases in human alveolar macrophages
Am. J. Respir. Cell Mol. Biol.
13
196-204
1995
Homo sapiens
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
Shariat-Madar, Z.; Mahdi, F.; Schmaier, A.H.
Recombinant prolylcarboxypeptidase activates plasma prekallikrein
Blood
15
4554-4561
2004
Homo sapiens
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Shariat-Madar, Z.; Mahdi, F.; Schmaier, A.H.
Recombinant prolylcarboxypeptidase activates plasma prekallikrein
Blood
103
4554-4561
2004
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Mallela, J.; Yang, J.; Shariat-Madar, Z.
Prolylcarboxypeptidase: A cardioprotective enzyme
Int. J. Biochem. Cell Biol.
41
477-481
2009
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Kehoe, K.; Brouns, R.; Verkerk, R.; Engelborghs, S.; De Deyn, P.; Hendriks, D.; De Meester, I.
Prolyl carboxypeptidase activity decline correlates with severity and short-term outcome in acute ischemic stroke
Neurochem. Res.
40
81-88
2014
Homo sapiens
Manually annotated by BRENDA team
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