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Information on EC 3.4.17.21 - Glutamate carboxypeptidase II and Organism(s) Homo sapiens and UniProt Accession Q04609

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.17 Metallocarboxypeptidases
                3.4.17.21 Glutamate carboxypeptidase II
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This record set is specific for:
Homo sapiens
UNIPROT: Q04609 not found.
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Word Map
  • 3.4.17.21
  • tomography
  • positron
  • metastases
  • psma-targeted
  • node
  • lncap
  • tracer
  • prostatectomy
  • castration-resistant
  • modal
  • radioligands
  • androgen
  • psma-positive
  • radiotherapy
  • radionuclide
  • 68ga-psma
  • biodistribution
  • radiotracers
  • neovasculature
  • radiopharmaceutical
  • mcrpc
  • theranostic
  • pelvic
  • gleason
  • psma-expressing
  • suvmax
  • restaging
  • oligometastatic
  • 68ga-labeled
  • multiparametric
  • urea-based
  • spect
  • dosimetry
  • scintigraphy
  • abiraterone
  • castrate-resistant
  • n-acetylaspartate
  • extraprostatic
  • mpmri
  • pet-ct
  • enzalutamide
  • 18f-labeled
  • positron-emission
  • tomography-computed
  • radium-223
  • pharmacology
  • radioimmunotherapy
  • medicine
  • tumor-to-background
  • analysis
  • radiometals
  • postprostatectomy
  • per-patient
  • diagnostics
  • drug development
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates
Synonyms
prostate-specific membrane antigen, gcpii, prostate specific membrane antigen, glutamate carboxypeptidase ii, naaladase, gcp ii, folh1, folate hydrolase, naag peptidase, n-acetylated alpha-linked acidic dipeptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
folate hydrolase
-
N-acetyl-alpha-linked acidic dipeptidase I
-
Naaladase I
-
Prostate-specific membrane antigen
-
100 kDa ileum brush border membrane protein
-
-
-
-
Acetylaspartylglutamate dipeptidase
-
-
-
-
Dipeptidase, acetylaspartylglutamate
-
-
-
-
FOLH1
-
-
Folylpoly-gamma-glutamate carboxypeptidase
-
-
-
-
folylpoly-gamma-glutamate carboxypeptidase II
-
-
glutamate carboxypeptidase
-
-
glutamate carboxypeptidase II
-
-
glutamate carboxypeptidase III
-
-
GPCPII
-
-
I100
-
-
-
-
Ileal dipeptidylpeptidase
-
-
-
-
Membrane glutamate carboxypeptidase
-
-
-
-
mGCP
-
-
-
-
N-acetylaspartylglutamate peptidase
-
-
N-Acetylated alpha-linked acidic dipeptidase
N-Acetylated-alpha-linked acidic dipeptidase
-
-
-
-
N-Acetylated-alpha-linked-acidic dipeptidase
-
-
-
-
N-Acetylated-alpha-linked-amino dipeptidase
-
-
-
-
NAADLADse
-
-
NAAG peptidase
-
-
NAAG-hydrolyzing activity
-
-
NAALA dipeptidase
-
-
-
-
NAALADase
prostate specific membrane antigen
-
-
Prostate-specific membrane antigen
Prostate-specific membrane antigen homolog
-
-
-
-
prostate-specificmembrane antigen
-
-
Prostrate-specific membrane antigen
-
-
-
-
PSM
-
-
-
-
PSM antigen
-
-
-
-
Pteroylpoly-gamma-glutamate carboxypeptidase
-
-
-
-
Rat NAAG peptidase
-
-
-
-
additional information
-
glutamate carboxypeptidase III and glutamate carboxypeptidase II belong to the transferrin receptor/glutamate carboxypeptidase II superfamily
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates
show the reaction diagram
release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates
show the reaction diagram
T640 is involved in catalysis, the N-glycosylation status is important for actalytic activity
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
PATHWAY SOURCE
PATHWAYS
CAS REGISTRY NUMBER
COMMENTARY hide
111070-04-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
amyloid-beta + H2O
?
show the reaction diagram
the enzyme has two distinctive binding sites for two different substrates. Amyloid-beta degradation occurs through S1 pocket but not through S1' pocket responsible for hydrolysis of N-acetyl-L-aspartyl-L-glutamate. Pre-incubation with N-acetyl-L-aspartyl-L-glutamate and amyloid-beta does not affect amyloid-beta degradation and hydrolysis of N-acetyl-L-aspartyl-L-glutamate, respectively
-
-
?
folyl-(gamma-L-glutamic acid)2 + H2O
folyl-gamma-L-glutamic acid + L-glutamate
show the reaction diagram
-
-
-
?
folyl-(gamma-L-glutamic acid)3 + H2O
folyl-(gamma-L-glutamic acid)2 + L-glutamate
show the reaction diagram
-
-
-
?
folyl-(gamma-L-glutamic acid)4 + H2O
folyl-(gamma-L-glutamic acid)3 + L-glutamate
show the reaction diagram
-
-
-
?
folyl-gamma-L-glutamic acid + H2O
folate + L-glutamate
show the reaction diagram
-
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
show the reaction diagram
N-acetyl-L-aspartyl-L-glutamate
N-acetyl-L-aspartate + L-glutamate
show the reaction diagram
-
-
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-Asp + L-Glu
show the reaction diagram
N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
show the reaction diagram
pteroyl-di-L-glutamate + H2O
L-Glu + pteroylglutamate
show the reaction diagram
-
-
-
?
folyl-poly-gamma-glutamate + H2O
?
show the reaction diagram
-
cleavage of the C-terminal glutamate
-
-
?
methotrexate triglutamate + H2O
L-Glu + methotrexate
show the reaction diagram
-
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
show the reaction diagram
N-acetyl-Asp-Glu + H2O
N-acetyl-Asp + Glu
show the reaction diagram
-
-
-
-
?
N-Acetyl-L-Asp-L-Glu + H2O
?
show the reaction diagram
-
functions as a cell surface peptidase, possibly hydrolzing peptides in prostatic fluid
-
-
?
N-Acetyl-L-Asp-L-Glu + H2O
N-Acetyl-L-Asp + L-Glu
show the reaction diagram
-
-
-
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
L-glutamate + N-acetyl-L-aspartate
show the reaction diagram
N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
show the reaction diagram
-
-
-
-
?
N-[4-(phenylazo)-benzoyl]-L-glutamyl-gamma-L-glutamic acid + H2O
?
show the reaction diagram
-
-
-
-
?
poly-gamma-glutamate folate + H2O
?
show the reaction diagram
poly-gamma-Glutamylfolate + H2O
L-Glu + gamma-glutamylfolate
show the reaction diagram
-
-
removes sequentially gamma-linked glutamates
?
pteroylpentaglutamate + H2O
L-Glu + pteroylglutamate
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
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
show the reaction diagram
N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
show the reaction diagram
folyl-poly-gamma-glutamate + H2O
?
show the reaction diagram
-
cleavage of the C-terminal glutamate
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
show the reaction diagram
N-acetyl-Asp-Glu + H2O
N-acetyl-Asp + Glu
show the reaction diagram
-
-
-
-
?
N-Acetyl-L-Asp-L-Glu + H2O
?
show the reaction diagram
-
functions as a cell surface peptidase, possibly hydrolzing peptides in prostatic fluid
-
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
L-glutamate + N-acetyl-L-aspartate
show the reaction diagram
N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
show the reaction diagram
-
-
-
-
?
poly-gamma-glutamate folate + H2O
?
show the reaction diagram
-
activity outside of the cell
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
even a slight disruption of the Ca2+-binding site destabilizes the three-dimensional fold of glutamate carboxypeptidase II and is associated with impaired secretion, a high propensity to form nonphysiological oligomers, and an inability to bind active site-targeted ligands. Additionally, the Ca2+-binding site is critical for maintenance of the native homodimeric quaternary arrangement of GCPII, which is indispensable for its enzymatic activity
Ca2+
-
positively regulates enzyme expression
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2S)-2-amino-3-(3,5-dioxo-1,2,4-oxadiazolidin-2-yl)propanoic acid
-
(S)-2-(3-((R)-1-carboxy-(2-methylthio)ethyl)ureido)pentanedioic acid
DCMC
(S)-2-(3-((R)-1-carboxy-2-(4-fluorobenzylthio)ethyl)ureido)pentanedioic acid
DCFBC
(S)-2-(3-((S)-1-carboxy-(4-iodobenzamido)pentyl)ureido)pentanedioic acid
(S)-2-(3-((S)-1-carboxy-2-(4-hydroxy-3-iodophenyl)ethyl)ureido)pentanedioic acid
DCIT
(S)-2-(3-((S)-1-carboxy-5-(1,2-dicarba-closo-dodecarboranylamido) pentyl)ureido)pentanedioic acid
-
(S)-2-(3-((S)-5-(6-(4-(4-(4-acetylpiperazin-1-yl)phenyl)piperazin-1-yl)-N-(4-bromobenzyl)nicotinamido)-1-carboxypentyl)ureido)-pentanedioic acid
4200fold selectivity compared to glutamate carboxypeptidase III
(S)-2-(3-((S)-5-(6-(4-(4-(4-acetylpiperazin-1-yl)phenyl)piperazin-1-yl)nicotinamido)-1-carboxypentyl)ureido)pentanedioic acid
1400fold selectivity compared to glutamate carboxypeptidase III
(S)-2-(3-((S)-5-(N-(4-bromobenzyl)-6-(4-(4-(4-(4-carboxy-3-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoyl)piperazin-1-yl)phenyl)-piperazin-1-yl)nicotinamido)-1-carboxypentyl)ureido)pentanedioic acid
1900fold selectivity compared to glutamate carboxypeptidase III
(S)-2-(3-((S)-5-(N-(4-bromobenzyl)-6-(4-(4-(4-(41-oxo-45-((3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)-4,7,10,13,16,19,22,25,28,31,34,37-dodecaoxa-40-azapentatetracontan-1-oyl)piperazin-1-yl)phenyl)piperazin-1-yl)nicotinamido)-1-carboxypentyl)ureido)pentanedioic acid
6600fold selectivity compared to glutamate carboxypeptidase III
2-(phosphonomethyl) pentanedioic acid
inhibitor completely blocks N-acetylaspartylglutamate cleavage activity but not Amyloid-beta degradation
2-(phosphonomethyl)-pentanedioic acid
i.e. 2-PMPA
2-(phosphonomethyl)pentandioic acid
10fold selectivity compared to glutamate carboxypeptidase III
2-(phosphonomethyl)pentanedioic acid
4-[(2-(R))-2-carboxy-5-(oxidanylamino)-5-oxidanylidene-pentyl]benzoic acid
-
4-[(2-(S))-2-carboxy-5-(oxidanylamino)-5-oxidanylidene-pentyl]benzoic acid
-
DKFZ-PSMA-11
720fold selectivity compared to glutamate carboxypeptidase III
N-(4-fluorobenzoyl)-L-isoleucyl-O-[[[(1S)-1,3-dicarboxypropyl]amino](hydroxy)phosphoryl]-L-serine
-
N-(4-fluorobenzoyl)-L-valyl-O-[[[(1S)-1,3-dicarboxypropyl]amino](hydroxy)phosphoryl]-L-serine
-
N-([(1S)-1-carboxy-5-([(4-iodophenyl)carbonyl]amino)pentyl]carbamoyl)-L-glutamic acid
P1'-diversified urea-based inhibitor, in complex with enzyme PDB entry 3D7H
N-2-([(1S)-1-carboxy-2-(furan-2-yl)ethyl]carbamoyl)-N-6-(4-iodobenzoyl)-L-lysine
P1'-diversified urea-based inhibitor, in complex with enzyme PDB entry 4OC3
N-2-([(1S)-1-carboxybut-3-yn-1-yl]carbamoyl)-N-6-(4-iodobenzoyl)-L-lysine
P1'-diversified urea-based inhibitor, in complex with enzyme PDB entry 4OC2
N-[(2-benzamidoethoxy)(hydroxy)phosphoryl]-L-glutamic acid
-
N-[4-carboxy-3-(carboxymethyl)-3-hydroxybutanoyl]-L-glutamic acid
-
N-[hydroxy(4-phenylbutoxy)phosphoryl]-L-glutamic acid
-
N-[[(1S)-1-carboxy-3-methylbutyl]carbamoyl]-L-glutamic acid
-
N-[[(1S)-1-carboxy-5-(4-iodobenzamido)pentyl]carbamoyl]-L-glutamic acid
-
N-[[(1S)-1-carboxy-5-([5-[3-(3-[[[2-[[[5-(2-carboxyethyl)-2-hydroxyphenyl]methyl](carboxymethyl)amino]ethyl](carboxymethyl)amino]methyl]-4-hydroxyphenyl)propanamido]pentanoyl]amino)pentyl]carbamoyl]-L-glutamic acid
-
N-[[(1S)-5-([(4-bromophenyl)methyl][6-[4-(4-[4-[4-carboxy-3-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoyl]piperazin-1-yl]phenyl)piperazin-1-yl]pyridine-3-carbony]amino)-1-carboxypentyl]carbamoyl]-L-glutamic acid
-
N-[[(1S)-5-acetamido-1-carboxypentyl]carbamoyl]-L-glutamic acid
-
N-[[(1S)-5-[acetyl[(4-bromophenyl)methyl]amino]-1-carboxypentyl]carbamoyl]-L-glutamic acid
-
N-[[(2R)-2-benzamido-2-carboxyethoxy](hydroxy)phosphoryl]-L-glutamic acid
-
N-[[(2S)-2-benzamido-2-carboxyethoxy](hydroxy)phosphoryl]-L-glutamic acid
-
N-[[(2S)-2-[[(6S)-6-amino-6-carboxy-3-oxohexyl]amino]-2-carboxyethoxy](hydroxy)phosphoryl]-L-glutamic acid
-
N-[[([1,1'-biphenyl]-4-yl)methoxy](hydroxy)phosphoryl]-L-glutamic acid
-
N-[[[(1S)-1-carboxy-3-methylbutyl]amino]carbonyl]-L-glutamic acid
i.e. ZJ-43. 160fold selectivity compared to glutamate carboxypeptidase III
(2S)-2-([hydroxy[2-(4-hydroxyphenyl)ethoxy]phosphoryl]methyl)pentanedioic acid
-
-
(2S)-2-([[2-(4-fluorophenyl)ethoxy](hydroxy)phosphoryl]methyl)pentanedioic acid
-
-
(2S)-2-([[2-(4-[[N-(tert-butoxycarbonyl)glycyl]amino]phenyl)ethoxy](hydroxy)phosphoryl]methyl)pentanedioic acid
-
-
(2S)-2-[([[(1S)-1,3-dicarboxypropyl]amino]carbonyl)amino]pentanedioic acid
-
-
(2S)-2-[([[(1S)-1-carboxy-2-(4-hydroxyphenyl)ethyl]amino]carbonyl)amino]pentanedioic acid
-
the inhibitor has the ability to reduce the perception of inflammatory pain
(2S)-2-[([[(1S)-1-carboxy-2-phenylethyl]amino]carbonyl)amino]pentanedioic acid
-
-
(2S)-2-[([[(1S)-1-carboxy-3-(1H-tetrazol-5-yl)propyl]amino]carbonyl)amino]pentanedioic acid
-
-
(2S)-2-[([[(1S)-1-carboxy-3-(2H-tetrazol-5-yl)propyl]amino]carbonyl)amino]-4-(2H-tetrazol-5-yl)butanoic acid
-
-
(2S)-2-[([[(1S)-3-carboxy-1-(2H-tetrazol-5-yl)propyl]amino]carbonyl)amino]pentanedioic acid
-
-
(2S)-2-[([[(S)-carboxy(4-hydroxyphenyl)methyl]amino]carbonyl)amino]pentanedioic acid
-
-
(2S)-2-[[(2-[4-[(tert-butoxycarbonyl)amino]phenyl]ethoxy)(hydroxy)phosphoryl]methyl]pentanedioic acid
-
-
(2S)-2-[[([(1S)-1-carboxy-3-[1-(2-cyanoethyl)-1H-tetrazol-5-yl]propyl]amino)carbonyl]amino]pentanedioic acid
-
-
(2S)-2-[[([(1S)-3-carboxy-1-[2-(2-cyanoethyl)-2H-tetrazol-5-yl]propyl]amino)carbonyl]amino]pentanedioic acid
-
-
(2S)-2-[[butyl(hydroxy)phosphorothioyl]amino]pentanedioic acid
-
-
(2S)-2-[[ethyl(hydroxy)phosphorothioyl]amino]pentanedioic acid
-
-
(2S)-2-[[hydroxy(2-phenylethoxy)phosphoryl]methyl]pentanedioic acid
-
-
(2S)-2-[[hydroxy(3-phenylpropoxy)phosphoryl]methyl]pentanedioic acid
-
-
(2S)-2-[[hydroxy(methyl)phosphorothioyl]amino]pentanedioic acid
-
-
(2S)-2-[[hydroxy(phenyl)phosphorothioyl]amino]pentanedioic acid
-
-
(2S)-2-[[hydroxy(phenyl)phosphorothioyl]oxy]pentanedioic acid
-
-
(2S)-2-[[hydroxy(phenyl)phosphoryl]amino]pentanedioic acid
-
-
(2S)-2-[[[2-[4-(acetylamino)phenyl]ethoxy](hydroxy)phosphoryl]methyl]pentanedioic acid
-
-
(2S,2'S,4R)-4-benzyl-N,N'-carbonyldiglutamic acid
-
-
(2S,2'S,4R,4'R)-4,4'-dibenzyl-N,N'-carbonyldiglutamic acid
-
-
(2S,2'S,4R,4'R)-N,N'-carbonyl-4,4'-dimethyldiglutamic acid
-
-
(2S,2'S,4S)-N,N'-carbonyl-4-methyldiglutamic acid
-
-
(2S,2'S,4S,4'S)-N,N'-carbonyl-4,4'-dimethyldiglutamic acid
-
-
(2S,3'S)-[[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl]-pentanedioic acid
-
EPE, a phosphapeptide transition state analog of glutamyl-glutamate
(2S,4R)-2-[([[(1S,3R)-1,3-dicarboxybutyl]amino]carbonyl)amino]-4-methylpentanedioic acid
-
-
(2S,4S)-2-[([[(1S,3S)-1,3-dicarboxybutyl]amino]carbonyl)amino]-4-methylpentanedioic acid
-
-
(4S)-4-[([[(1S)-3-carboxy-1-(2H-tetrazol-5-yl)propyl]amino]carbonyl)amino]-4-(2H-tetrazol-5-yl)butanoic acid
-
-
(9S,13S)-1-(3-iodophenyl)-3,11-dioxo-2,4,10,12-tetraazapentadecane-9,13,15-tricarboxylic acid
-
-
(R)-2-(3-mercaptopropyl)-pentanedioic acid
-
equally potent as the S-isomer, 0.000085 mM
(R)-2-(hydroxypentafluorophenylmethyl-phosphinoylmethyl)pentanedioic acid
-
40fold less potent than the S-isomer, IC50: 0.0014 mM
(R)-2-(phosphonomethyl)-pentanedioic acid
-
less potent than the S-isomer, IC50: 0.000030 mM
(S)-2-(3-((S)-1-carboxy-2-(4-hydroxy-3-iodophenyl)ethyl)ureido)pentanedioic acid
-
DCIT
(S)-2-(3-((S)-1-carboxy-5-(2-chlorobenzylamino)pentyl)ureido)pentanedioic acid
-
-
(S)-2-(3-((S)-1-carboxy-5-(2-iodobenzylamino)pentyl)ureido)-pentanedioic acid
-
-
(S)-2-(3-((S)-1-carboxy-5-(3-(4-bromophenyl)ureido)pentyl)ureido)pentanedioic acid
-
-
(S)-2-(3-((S)-1-carboxy-5-(3-(4-chlorophenyl)ureido)pentyl)ureido)pentanedioic acid
-
-
(S)-2-(3-((S)-1-carboxy-5-(3-(4-fluorophenyl)ureido)pentyl)ureido)pentanedioic acid
-
-
(S)-2-(3-((S)-1-carboxy-5-(3-(4-iodophenyl)ureido)pentyl)ureido)pentanedioic acid
(S)-2-(3-((S)-1-carboxy-5-(3-chlorobenzylamino)pentyl)ureido)pentanedioic acid
-
-
(S)-2-(3-((S)-1-carboxy-5-(3-iodobenzylamino)pentyl)ureido)-pentanedioic acid
-
-
(S)-2-(3-((S)-1-carboxy-5-(3-phenylureido)pentyl)ureido)pentanedioic acid
-
-
(S)-2-(3-((S)-1-carboxy-5-(4-bromobenzylamino)pentyl)ureido)pentanedioic acid
-
-
(S)-2-(3-((S)-1-carboxy-5-(4-chlorobenzylamino)pentyl)ureido)pentanedioic acid
-
-
(S)-2-(3-((S)-1-carboxy-5-(4-fluorobenzylamino)pentyl)ureido)pentanedioic acid
-
-
(S)-2-(3-((S)-1-carboxy-5-(4-iodobenzylamino)pentyl)ureido)-pentanedioic acid
-
-
(S)-2-(3-((S)-1-carboxy-5-(4-iodobenzylamino)pentyl)ureido)pentanedioic acid
-
i.e. MIP-1072, the compound shows affinity to and uptake into prostate cancer cells, binding analysis, overview
(S)-2-(3-((S)-1-carboxy-5-(4-iodophenylsulfonamido)pentyl)-ureido)pentanedioic acid
-
-
(S)-2-(3-((S)-1-carboxy-5-(naphthalen-1-ylmethylamino)pentyl)-ureido)pentanedioic acid
-
-
(S)-2-(3-((S)-5-(benzylamino)-1-carboxypentyl)ureido)pentanedioic acid
-
-
(S)-2-(3-((S)-5-amino-1-carboxypentyl)ureido)pentanedioic acid
-
-
(S)-2-(3-(4-iodobenzyl)ureido)pentanedioic acid
-
-
(S)-2-(3-mercaptopropyl)-pentanedioic acid
-
equally potent as the R-isomer, 0.000067 mM
(S)-2-(hydroxypentafluorophenylmethyl-phosphinoylmethyl)pentanedioic acid
-
40fold more potent than the R-isomer, IC50: 0.000034 mM
(S)-2-(phosphonomethyl)-pentanedioic acid
-
more potent than the R-isomer, IC50: 0.0000001 mM
(S)-2-[3-((S)-1-carboxy-2-(4-hydroxyphenyl)ethyl)ureido]pentanedioic acid
(S)-2-[3-((S)-1-carboxy-2-phenylethyl)ureido]pentanedioic acid
-
-
(S)-2-[3-((S)-1-carboxy-3-(1H-tetrazol-5-yl)propyl)ureido]pentanedioic acid
(S)-2-[3-((S)-1-carboxy-3-(methylsulfanyl)propyl)ureido]pentanedioic acid
-
i.e. inhibitor ZJ11
(S)-2-[3-((S)-1-carboxy-3-methylbutyl)ureido]pentanedioic acid
-
i.e. inhibitor ZJ43
(S)-2-[3-((S)-1-carboxy-3-[1-(2-cyanoethyl)-1H-tetrazol-5-yl]propyl)ureido]pentanedioic acid
-
-
(S)-2-[3-((S)-3-carboxy-1-(1H-tetrazol-5-yl)propyl)ureido]pentanedioic acid
-
-
(S)-2-[3-((S)-3-carboxy-1-[1-(2-cyanoethyl)-1H-tetrazol-5-yl]propyl)ureido]pentanedioic acid
-
-
(S)-2-[3-((S)-alpha-carboxy-4-hydroxybenzyl)ureido]pentanedioic acid
-
-
(S)-2-[3-((S)-alpha-carboxybenzyl)ureido]pentanedioic acid
-
-
(S)-2-[3-(S)-(1,3-dicarboxypropyl)ureido]pentanedioinc acid
-
-
(S,S)-4,4'-bis[1-(2-cyanoethyl)-1H-tetrazol-5-yl]-2,2'-ureylenedibutyric acid
-
-
(S,S)-4,4'-bis[1-(2-cyanoethyl)-1H-tetrazol-5-yl]-4,4'-ureylenedibutyric acid
-
-
(S,S)-4,4'-di-(1H-tetrazol-5-yl)-2,2'-ureylenedibutyric acid
-
-
(S,S)-4,4'-di-(1H-tetrazol-5-yl)-4,4'-ureylenedibutyric acid
-
-
(S,S)-N,N'-carbonyl-2,2'-dimethyldiglutamic acid
-
-
2-(2-carboxy-5-mercaptopentyl)benzoic acid
-
IC50: 1700 nM
2-(3-carbamoylbenzyl)-5-mercaptopentanoic acid
-
IC50: 2200 nM
2-(3-carboxybenyl)succinic acid
-
IC50: 0.015 mM
2-(3-cyanobenzyl)-5-mercaptopentanoic acid
-
IC50: 1800 nM
2-(3-mercaptopropyl)-pentanedioic acid
2-(phosphonomethyl)-pentanedioic acid
2-(phosphonomethyl)pentanedioic acid
2-amino-3-(3,5-dioxo[1,2,4]oxadiazolidin-2-yl)propionic acid
-
i.e. quisqualic acid, a glutamate-like inhibitor of GCPIII and GCPII
2-benzyl-5-mercaptopentanoic acid
-
IC50: 1400 nM
3-(1-carboxy-4-mercaptobutoxy)benzoic acid
-
IC50: 14 nM
3-(2-carbamoyl-5-mercaptopentyl)benzoic acid
-
IC50: 640 nM
3-(2-carboxy-3-hydroxycarbamoylpropyl)benzoic acid
-
IC50: 0.015 mM
3-(2-carboxy-3-phosphonopropyl)benzoic acid
-
IC50: 120 nM
3-(2-carboxy-5-mercaptopentyl)benzoic acid
-
IC50: 15 nM
3-(2-carboxy-5-mercaptopentyl)benzoic acid methyl ester
-
IC50: 2700 nM
3-(2-carboxy-5-mercaptosulfanylpentyl)benzoic acid
-
IC50: 0.02 mM
3-(2-carboxy-5-tritylsulfanylpentyl)benzoic acid
-
IC50: 0.02 mM
3-(5-mercapto-2-methoxycarbonylpentyl)benzoic acid
-
IC50: 730 nM
3-[(1-carboxy-4-mercaptobutyl)thio]benzoic acid
-
IC50: 32 nM
3-[2-carboxy-3-(hydroxypentafluorophenylmethylphosphinoyl)propyl]benzoic acid
-
IC50: 2400 nM
4,4'-phosphinicobis(butane-1,3-dicarboxylic acid)
-
i.e. PBDA, effects of stereoisomers, overview
4-(2-carboxy-5-mercaptopentyl)benzoic acid
-
IC50: 63 nM
diazabicycloalkane
-
cis- and trans-isomers, dipeptide mimetic
-
diphenyl 2-[[[2-[4-([[7-(diethylamino)-2-oxo-2H-chromen-3-yl]carbamoyl]amino)phenyl]ethoxy](hydroxy)phosphoryl]methyl]pentanedioate
-
-
DUPA
-
enzyme active site binding structure, docking and modelling, detailed overview
GPI 5693
-
i.e. (R,S)-2-(3-mercaptopropyl)-pentanedioic acid or 2-MPPA, pharmacokinetics and safety of the NAALADase-inhibitor and its effects on the central nervous system after application in vivo, overview
GPI-18431
-
enzyme active site binding structure, docking and modelling, detailed overview
GPI5232
L-Glu
-
-
MOPS
-
-
N-(tert-butoxycarbonyl)glycyl-N-[4-[2-([[(2S)-2,4-dicarboxybutyl](hydroxy)phosphoryl]oxy)ethyl]phenyl]-L-prolinamide
-
-
N-(tert-butoxycarbonyl)glycylglycyl-N-[4-[2-([[(2S)-2,4-dicarboxybutyl](hydroxy)phosphoryl]oxy)ethyl]phenyl]glycinamide
-
-
N-Acetyl-beta-L-Asp-L-Glu
-
-
N-[[(1S)-1-carboxy-2-(4-hydroxyphenyl)ethyl]carbamoyl]-L-glutamic acid
-
i.e. inhibitor ZJ17, antinociceptive effect of the inhibitor in the rat formalin test and the rat neuropathic pain model, overview
N-[[(1S)-1-carboxy-3-(methylsulfanyl)propyl]carbamoyl]-L-glutamic acid
-
i.e. inhibitor ZJ11, antinociceptive effect of the inhibitor in the rat formalin test and the rat neuropathic pain model, overview
N-[[(1S)-1-carboxy-3-methylbutyl]carbamoyl]-L-glutamic acid
-
i.e. inhibitor ZJ43, antinociceptive effect of the inhibitor in the rat formalin test and the rat neuropathic pain model, overview
pyropheophorbide-a conjugate
-
i.e. Ppa-2 conjugate, non-specificity of unconjugated Ppa, conjugation of a peptidomimetic inhibitor of PSMA to the porphyrinic PS, pyropheophorbide-a gives
Quisqualic acid
-
-
S-2-((2-(S-4-(4-18F-fluorobenzamido)-4-carboxybutanamido)-S-2-carboxyethoxy)hydroxyphosphorylamino)-pentanedioic acid
-
-
S-2-((2-(S-4-amino-4-carboxybutanamido)-S-2-carboxyethoxy)-hydroxyphosphorylamino)-pentanedioic acid
-
phosphoramidate
VA-033
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00055
N-acetyl-L-aspartyl-L-glutamate
pH 7.4, 37°C
0.000039
pteroyl-di-L-glutamate
pH 7.4, 37°C
0.000066 - 0.000334
N-acetyl-alpha-L-aspartyl-L-glutamate
130
N-acetyl-Asp-Glu
-
pH 7.4, 37°C
0.065
N-Acetyl-L-Asp-L-Glu
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1 - 1.45
N-acetyl-L-aspartyl-L-glutamate
5.09
pteroyl-di-L-glutamate
pH 7.4, 37°C
4
N-acetyl-Asp-Glu
-
pH 7.4, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2900
N-acetyl-L-aspartyl-L-glutamate
pH 7.4, 37°C
130513
pteroyl-di-L-glutamate
pH 7.4, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00052
(2S)-2-amino-3-(3,5-dioxo-1,2,4-oxadiazolidin-2-yl)propanoic acid
37°C, pH 7.4
0.000000003
(S)-2-(3-((S)-1-carboxy-(4-iodobenzamido)pentyl)ureido)pentanedioic acid
pH and temperature not specified in the publication
0.000000049
(S)-2-(3-((S)-5-(6-(4-(4-(4-acetylpiperazin-1-yl)phenyl)piperazin-1-yl)-N-(4-bromobenzyl)nicotinamido)-1-carboxypentyl)ureido)-pentanedioic acid
pH and temperature not specified in the publication
0.000000071
(S)-2-(3-((S)-5-(6-(4-(4-(4-acetylpiperazin-1-yl)phenyl)piperazin-1-yl)nicotinamido)-1-carboxypentyl)ureido)pentanedioic acid
pH and temperature not specified in the publication
0.0000000086
(S)-2-(3-((S)-5-(N-(4-bromobenzyl)-6-(4-(4-(4-(4-carboxy-3-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoyl)piperazin-1-yl)phenyl)-piperazin-1-yl)nicotinamido)-1-carboxypentyl)ureido)pentanedioic acid
pH and temperature not specified in the publication
0.00000011
(S)-2-(3-((S)-5-(N-(4-bromobenzyl)-6-(4-(4-(4-(41-oxo-45-((3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)-4,7,10,13,16,19,22,25,28,31,34,37-dodecaoxa-40-azapentatetracontan-1-oyl)piperazin-1-yl)phenyl)piperazin-1-yl)nicotinamido)-1-carboxypentyl)ureido)pentanedioic acid
pH and temperature not specified in the publication
0.00000028
2-(phosphonomethyl)pentandioic acid
pH and temperature not specified in the publication
0.00000026
2-(phosphonomethyl)pentanedioic acid
37°C, pH 7.4
0.000000018
DKFZ-PSMA-11
pH and temperature not specified in the publication
0.00000001
N-([(1S)-1-carboxy-5-([(4-iodophenyl)carbonyl]amino)pentyl]carbamoyl)-L-glutamic acid
pH not specified in the publication, temperature not specified in the publication
0.0000053
N-2-([(1S)-1-carboxy-2-(furan-2-yl)ethyl]carbamoyl)-N-6-(4-iodobenzoyl)-L-lysine
pH not specified in the publication, temperature not specified in the publication
0.0000053
N-2-([(1S)-1-carboxybut-3-yn-1-yl]carbamoyl)-N-6-(4-iodobenzoyl)-L-lysine
pH not specified in the publication, temperature not specified in the publication
0.016
N-[4-carboxy-3-(carboxymethyl)-3-hydroxybutanoyl]-L-glutamic acid
37°C, pH 7.4
0.00000058
N-[[(1S)-1-carboxy-3-methylbutyl]carbamoyl]-L-glutamic acid
37°C, pH 7.4
0.000000017
N-[[(1S)-1-carboxy-5-(4-iodobenzamido)pentyl]carbamoyl]-L-glutamic acid
37°C, pH 7.4
0.000000018
N-[[(1S)-1-carboxy-5-([5-[3-(3-[[[2-[[[5-(2-carboxyethyl)-2-hydroxyphenyl]methyl](carboxymethyl)amino]ethyl](carboxymethyl)amino]methyl]-4-hydroxyphenyl)propanamido]pentanoyl]amino)pentyl]carbamoyl]-L-glutamic acid
37°C, pH 7.4
0.000000021
N-[[(1S)-5-([(4-bromophenyl)methyl][6-[4-(4-[4-[4-carboxy-3-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoyl]piperazin-1-yl]phenyl)piperazin-1-yl]pyridine-3-carbony]amino)-1-carboxypentyl]carbamoyl]-L-glutamic acid
37°C, pH 7.4
0.00000017
N-[[(1S)-5-acetamido-1-carboxypentyl]carbamoyl]-L-glutamic acid
37°C, pH 7.4
0.00000005
N-[[(1S)-5-[acetyl[(4-bromophenyl)methyl]amino]-1-carboxypentyl]carbamoyl]-L-glutamic acid
37°C, pH 7.4
0.00000058
N-[[[(1S)-1-carboxy-3-methylbutyl]amino]carbonyl]-L-glutamic acid
pH and temperature not specified in the publication
0.000008
(2S)-2-[([[(1S)-1,3-dicarboxypropyl]amino]carbonyl)amino]pentanedioic acid
-
pH 7.4, 37°C
0.000003
(2S)-2-[([[(1S)-1-carboxy-2-(4-hydroxyphenyl)ethyl]amino]carbonyl)amino]pentanedioic acid
-
pH 7.4, 37°C
0.000012
(2S)-2-[([[(1S)-1-carboxy-2-phenylethyl]amino]carbonyl)amino]pentanedioic acid
-
pH 7.4, 37°C
0.0000009
(2S)-2-[([[(1S)-1-carboxy-3-(1H-tetrazol-5-yl)propyl]amino]carbonyl)amino]pentanedioic acid
-
pH 7.4, 37°C
0.0000149
(2S)-2-[([[(1S)-1-carboxy-3-(2H-tetrazol-5-yl)propyl]amino]carbonyl)amino]-4-(2H-tetrazol-5-yl)butanoic acid
-
pH 7.4, 37°C
0.000335
(2S)-2-[([[(1S)-3-carboxy-1-(2H-tetrazol-5-yl)propyl]amino]carbonyl)amino]pentanedioic acid
-
pH 7.4, 37°C
0.0000059
(2S)-2-[([[(S)-carboxy(4-hydroxyphenyl)methyl]amino]carbonyl)amino]pentanedioic acid
-
pH 7.4, 37°C
0.0000053
(2S)-2-[[([(1S)-1-carboxy-3-[1-(2-cyanoethyl)-1H-tetrazol-5-yl]propyl]amino)carbonyl]amino]pentanedioic acid
-
pH 7.4, 37°C
0.002711
(2S)-2-[[([(1S)-3-carboxy-1-[2-(2-cyanoethyl)-2H-tetrazol-5-yl]propyl]amino)carbonyl]amino]pentanedioic acid
-
pH 7.4, 37°C
0.000104
(2S)-2-[[butyl(hydroxy)phosphorothioyl]amino]pentanedioic acid
-
pH 7.4, 37°C
0.00109
(2S)-2-[[ethyl(hydroxy)phosphorothioyl]amino]pentanedioic acid
-
pH 7.4, 37°C
0.000719
(2S)-2-[[hydroxy(methyl)phosphorothioyl]amino]pentanedioic acid
-
pH 7.4, 37°C
0.00639
(2S)-2-[[hydroxy(phenyl)phosphorothioyl]amino]pentanedioic acid
-
pH 7.4, 37°C
0.0146
(2S)-2-[[hydroxy(phenyl)phosphorothioyl]oxy]pentanedioic acid
-
pH 7.4, 37°C
0.00111
(2S)-2-[[hydroxy(phenyl)phosphoryl]amino]pentanedioic acid
-
pH 7.4, 37°C
0.000095 - 0.0000953
(2S,2'S,4R)-4-benzyl-N,N'-carbonyldiglutamic acid
0.000392
(2S,2'S,4R,4'R)-4,4'-dibenzyl-N,N'-carbonyldiglutamic acid
0.00129
(2S,2'S,4R,4'R)-N,N'-carbonyl-4,4'-dimethyldiglutamic acid
-
pH 7.4, 37°C, recombinant enzyme
0.000014 - 0.0000144
(2S,2'S,4S)-N,N'-carbonyl-4-methyldiglutamic acid
0.00111
(2S,2'S,4S,4'S)-N,N'-carbonyl-4,4'-dimethyldiglutamic acid
-
pH 7.4, 37°C, recombinant enzyme
0.0000129 - 0.0000346
(2S,3'S)-[[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl]-pentanedioic acid
0.001285
(2S,4R)-2-[([[(1S,3R)-1,3-dicarboxybutyl]amino]carbonyl)amino]-4-methylpentanedioic acid
-
pH 7.4, 37°C
0.001109
(2S,4S)-2-[([[(1S,3S)-1,3-dicarboxybutyl]amino]carbonyl)amino]-4-methylpentanedioic acid
-
pH 7.4, 37°C
0.004388
(4S)-4-[([[(1S)-3-carboxy-1-(2H-tetrazol-5-yl)propyl]amino]carbonyl)amino]-4-(2H-tetrazol-5-yl)butanoic acid
-
pH 7.4, 37°C
0.0000015
(S)-2-(3-((S)-1-carboxy-2-(4-hydroxy-3-iodophenyl)ethyl)ureido)pentanedioic acid
-
-
0.00000024
(S)-2-(3-((S)-1-carboxy-5-(3-(4-iodophenyl)ureido)pentyl)ureido)pentanedioic acid
-
-
0.0000046
(S)-2-(3-((S)-1-carboxy-5-(4-iodobenzylamino)pentyl)ureido)pentanedioic acid
-
-
0.000003
(S)-2-[3-((S)-1-carboxy-2-(4-hydroxyphenyl)ethyl)ureido]pentanedioic acid
-
pH 7.4, 37°C, recombinant enzyme
0.000012
(S)-2-[3-((S)-1-carboxy-2-phenylethyl)ureido]pentanedioic acid
-
pH 7.4, 37°C, recombinant enzyme
0.0000009
(S)-2-[3-((S)-1-carboxy-3-(1H-tetrazol-5-yl)propyl)ureido]pentanedioic acid
-
pH 7.4, 37°C, recombinant enzyme
0.0000053
(S)-2-[3-((S)-1-carboxy-3-[1-(2-cyanoethyl)-1H-tetrazol-5-yl]propyl)ureido]pentanedioic acid
-
pH 7.4, 37°C, recombinant enzyme
0.000335
(S)-2-[3-((S)-3-carboxy-1-(1H-tetrazol-5-yl)propyl)ureido]pentanedioic acid
-
pH 7.4, 37°C, recombinant enzyme
0.00271
(S)-2-[3-((S)-3-carboxy-1-[1-(2-cyanoethyl)-1H-tetrazol-5-yl]propyl)ureido]pentanedioic acid
-
pH 7.4, 37°C, recombinant enzyme
0.0000059
(S)-2-[3-((S)-alpha-carboxy-4-hydroxybenzyl)ureido]pentanedioic acid
-
pH 7.4, 37°C, recombinant enzyme
0.0000021
(S)-2-[3-((S)-alpha-carboxybenzyl)ureido]pentanedioic acid
0.000008
(S)-2-[3-(S)-(1,3-dicarboxypropyl)ureido]pentanedioinc acid
-
pH 7.4, 37°C, recombinant enzyme
0.00443 - 0.004434
(S,S)-4,4'-bis[1-(2-cyanoethyl)-1H-tetrazol-5-yl]-2,2'-ureylenedibutyric acid
1
(S,S)-4,4'-bis[1-(2-cyanoethyl)-1H-tetrazol-5-yl]-4,4'-ureylenedibutyric acid
-
above, pH 7.4, 37°C, recombinant enzyme
0.000015
(S,S)-4,4'-di-(1H-tetrazol-5-yl)-2,2'-ureylenedibutyric acid
-
pH 7.4, 37°C, recombinant enzyme
0.00439
(S,S)-4,4'-di-(1H-tetrazol-5-yl)-4,4'-ureylenedibutyric acid
-
pH 7.4, 37°C, recombinant enzyme
0.000939
(S,S)-N,N'-carbonyl-2,2'-dimethyldiglutamic acid
0.00003
2-(3-mercaptopropyl)-pentanedioic acid
-
-
0.0000002 - 0.0000014
2-(phosphonomethyl)-pentanedioic acid
0.0000002 - 0.0000014
2-(phosphonomethyl)pentanedioic acid
0.00023 - 0.00102
2-amino-3-(3,5-dioxo[1,2,4]oxadiazolidin-2-yl)propionic acid
0.000008
DUPA
-
-
0.00003
GPI-18431
-
-
0.27 - 0.428
L-Glu
0.0000149
N-[[(1S)-1-carboxy-3-(1H-tetrazol-5-yl)propyl]carbamoyl]-L-glutamic acid
-
pH 7.4, 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000017
(S)-2-(3-((R)-1-carboxy-(2-methylthio)ethyl)ureido)pentanedioic acid
Homo sapiens
-
0.000014
(S)-2-(3-((R)-1-carboxy-2-(4-fluorobenzylthio)ethyl)ureido)pentanedioic acid
Homo sapiens
-
0.00000006
(S)-2-(3-((S)-1-carboxy-(4-iodobenzamido)pentyl)ureido)pentanedioic acid
Homo sapiens
-
0.0000005
(S)-2-(3-((S)-1-carboxy-2-(4-hydroxy-3-iodophenyl)ethyl)ureido)pentanedioic acid
Homo sapiens
-
0.000016
N-(4-fluorobenzoyl)-L-isoleucyl-O-[[[(1S)-1,3-dicarboxypropyl]amino](hydroxy)phosphoryl]-L-serine
Homo sapiens
37°C, pH 7.4
0.000016
N-(4-fluorobenzoyl)-L-valyl-O-[[[(1S)-1,3-dicarboxypropyl]amino](hydroxy)phosphoryl]-L-serine
Homo sapiens
37°C, pH 7.4
0.0018
N-[(2-benzamidoethoxy)(hydroxy)phosphoryl]-L-glutamic acid
Homo sapiens
37°C, pH 7.4
0.00018
N-[hydroxy(4-phenylbutoxy)phosphoryl]-L-glutamic acid
Homo sapiens
37°C, pH 7.4
0.0007
N-[[(2R)-2-benzamido-2-carboxyethoxy](hydroxy)phosphoryl]-L-glutamic acid
Homo sapiens
37°C, pH 7.4
0.000035
N-[[(2S)-2-benzamido-2-carboxyethoxy](hydroxy)phosphoryl]-L-glutamic acid
Homo sapiens
37°C, pH 7.4
0.000014
N-[[(2S)-2-[[(6S)-6-amino-6-carboxy-3-oxohexyl]amino]-2-carboxyethoxy](hydroxy)phosphoryl]-L-glutamic acid
Homo sapiens
37°C, pH 7.4
0.000168
N-[[([1,1'-biphenyl]-4-yl)methoxy](hydroxy)phosphoryl]-L-glutamic acid
Homo sapiens
37°C, pH 7.4
0.0000002
(2S)-2-([hydroxy[2-(4-hydroxyphenyl)ethoxy]phosphoryl]methyl)pentanedioic acid
Homo sapiens
-
-
0.0003
(2S)-2-([[2-(4-fluorophenyl)ethoxy](hydroxy)phosphoryl]methyl)pentanedioic acid
Homo sapiens
-
-
0.0000007
(2S)-2-([[2-(4-[[N-(tert-butoxycarbonyl)glycyl]amino]phenyl)ethoxy](hydroxy)phosphoryl]methyl)pentanedioic acid
Homo sapiens
-
-
0.0000001
(2S)-2-[[(2-[4-[(tert-butoxycarbonyl)amino]phenyl]ethoxy)(hydroxy)phosphoryl]methyl]pentanedioic acid
Homo sapiens
-
-
0.0000008
(2S)-2-[[hydroxy(2-phenylethoxy)phosphoryl]methyl]pentanedioic acid
Homo sapiens
-
-
0.000004
(2S)-2-[[hydroxy(3-phenylpropoxy)phosphoryl]methyl]pentanedioic acid
Homo sapiens
-
-
0.000004
(2S)-2-[[[2-[4-(acetylamino)phenyl]ethoxy](hydroxy)phosphoryl]methyl]pentanedioic acid
Homo sapiens
-
-
0.000018
(9S,13S)-1-(3-iodophenyl)-3,11-dioxo-2,4,10,12-tetraazapentadecane-9,13,15-tricarboxylic acid
Homo sapiens
-
-
0.0014
(R)-2-(hydroxypentafluorophenylmethyl-phosphinoylmethyl)pentanedioic acid
Homo sapiens
-
40fold less potent than the S-isomer, IC50: 0.0014 mM
0.00003
(R)-2-(phosphonomethyl)-pentanedioic acid
Homo sapiens
-
less potent than the S-isomer, IC50: 0.000030 mM
0.000245
(S)-2-(3-((S)-1-carboxy-5-(2-chlorobenzylamino)pentyl)ureido)pentanedioic acid
Homo sapiens
-
-
0.000037
(S)-2-(3-((S)-1-carboxy-5-(2-iodobenzylamino)pentyl)ureido)-pentanedioic acid
Homo sapiens
-
-
0.000002
(S)-2-(3-((S)-1-carboxy-5-(3-(4-bromophenyl)ureido)pentyl)ureido)pentanedioic acid
Homo sapiens
-
-
0.000004
(S)-2-(3-((S)-1-carboxy-5-(3-(4-chlorophenyl)ureido)pentyl)ureido)pentanedioic acid
Homo sapiens
-
-
0.000003
(S)-2-(3-((S)-1-carboxy-5-(3-(4-fluorophenyl)ureido)pentyl)ureido)pentanedioic acid
Homo sapiens
-
-
0.00001
(S)-2-(3-((S)-1-carboxy-5-(3-(4-iodophenyl)ureido)pentyl)ureido)pentanedioic acid
Homo sapiens
-
-
0.000277
(S)-2-(3-((S)-1-carboxy-5-(3-chlorobenzylamino)pentyl)ureido)pentanedioic acid
Homo sapiens
-
-
0.000443
(S)-2-(3-((S)-1-carboxy-5-(3-iodobenzylamino)pentyl)ureido)-pentanedioic acid
Homo sapiens
-
-
0.000012
(S)-2-(3-((S)-1-carboxy-5-(3-phenylureido)pentyl)ureido)pentanedioic acid
Homo sapiens
-
-
0.000043
(S)-2-(3-((S)-1-carboxy-5-(4-bromobenzylamino)pentyl)ureido)pentanedioic acid
Homo sapiens
-
-
0.000002
(S)-2-(3-((S)-1-carboxy-5-(4-chlorobenzylamino)pentyl)ureido)pentanedioic acid
Homo sapiens
-
-
0.0012
(S)-2-(3-((S)-1-carboxy-5-(4-fluorobenzylamino)pentyl)ureido)pentanedioic acid
Homo sapiens
-
-
0.000022
(S)-2-(3-((S)-1-carboxy-5-(4-iodobenzylamino)pentyl)ureido)-pentanedioic acid
Homo sapiens
-
-
0.00001
(S)-2-(3-((S)-1-carboxy-5-(4-iodophenylsulfonamido)pentyl)-ureido)pentanedioic acid
Homo sapiens
-
-
0.000154
(S)-2-(3-((S)-1-carboxy-5-(naphthalen-1-ylmethylamino)pentyl)-ureido)pentanedioic acid
Homo sapiens
-
-
0.00296
(S)-2-(3-((S)-5-(benzylamino)-1-carboxypentyl)ureido)pentanedioic acid
Homo sapiens
-
-
0.000498
(S)-2-(3-((S)-5-amino-1-carboxypentyl)ureido)pentanedioic acid
Homo sapiens
-
-
0.003
(S)-2-(3-(4-iodobenzyl)ureido)pentanedioic acid
Homo sapiens
-
-
0.000034
(S)-2-(hydroxypentafluorophenylmethyl-phosphinoylmethyl)pentanedioic acid
Homo sapiens
-
40fold more potent than the R-isomer, IC50: 0.000034 mM
0.0000001
(S)-2-(phosphonomethyl)-pentanedioic acid
Homo sapiens
-
more potent than the R-isomer, IC50: 0.0000001 mM
0.0017
2-(2-carboxy-5-mercaptopentyl)benzoic acid
Homo sapiens
-
IC50: 1700 nM
0.0022
2-(3-carbamoylbenzyl)-5-mercaptopentanoic acid
Homo sapiens
-
IC50: 2200 nM
0.015
2-(3-carboxybenyl)succinic acid
Homo sapiens
-
IC50: 0.015 mM
0.0018
2-(3-cyanobenzyl)-5-mercaptopentanoic acid
Homo sapiens
-
IC50: 1800 nM
0.00009
2-(3-mercaptopropyl)-pentanedioic acid
Homo sapiens
-
i.e. 2-MPPA, IC50: 90 nM
0.0000004
2-(phosphonomethyl)pentanedioic acid
Homo sapiens
-
-
0.0014
2-benzyl-5-mercaptopentanoic acid
Homo sapiens
-
IC50: 1400 nM
0.000014
3-(1-carboxy-4-mercaptobutoxy)benzoic acid
Homo sapiens
-
IC50: 14 nM
0.00064
3-(2-carbamoyl-5-mercaptopentyl)benzoic acid
Homo sapiens
-
IC50: 640 nM
0.015
3-(2-carboxy-3-hydroxycarbamoylpropyl)benzoic acid
Homo sapiens
-
IC50: 0.015 mM
0.00012
3-(2-carboxy-3-phosphonopropyl)benzoic acid
Homo sapiens
-
IC50: 120 nM
0.000015
3-(2-carboxy-5-mercaptopentyl)benzoic acid
Homo sapiens
-
IC50: 15 nM
0.0027
3-(2-carboxy-5-mercaptopentyl)benzoic acid methyl ester
Homo sapiens
-
IC50: 2700 nM
0.02
3-(2-carboxy-5-mercaptosulfanylpentyl)benzoic acid
Homo sapiens
-
IC50: 0.02 mM
0.02
3-(2-carboxy-5-tritylsulfanylpentyl)benzoic acid
Homo sapiens
-
IC50: 0.02 mM
0.00073
3-(5-mercapto-2-methoxycarbonylpentyl)benzoic acid
Homo sapiens
-
IC50: 730 nM
0.000032
3-[(1-carboxy-4-mercaptobutyl)thio]benzoic acid
Homo sapiens
-
IC50: 32 nM
0.0024
3-[2-carboxy-3-(hydroxypentafluorophenylmethylphosphinoyl)propyl]benzoic acid
Homo sapiens
-
IC50: 2400 nM
0.000063
4-(2-carboxy-5-mercaptopentyl)benzoic acid
Homo sapiens
-
IC50: 63 nM
0.000002
diphenyl 2-[[[2-[4-([[7-(diethylamino)-2-oxo-2H-chromen-3-yl]carbamoyl]amino)phenyl]ethoxy](hydroxy)phosphoryl]methyl]pentanedioate
Homo sapiens
-
-
0.000007
N-(tert-butoxycarbonyl)glycyl-N-[4-[2-([[(2S)-2,4-dicarboxybutyl](hydroxy)phosphoryl]oxy)ethyl]phenyl]-L-prolinamide
Homo sapiens
-
-
0.000008
N-(tert-butoxycarbonyl)glycylglycyl-N-[4-[2-([[(2S)-2,4-dicarboxybutyl](hydroxy)phosphoryl]oxy)ethyl]phenyl]glycinamide
Homo sapiens
-
-
0.000102
pyropheophorbide-a conjugate
Homo sapiens
-
pH 7.4, 37°C
0.000014
S-2-((2-(S-4-(4-18F-fluorobenzamido)-4-carboxybutanamido)-S-2-carboxyethoxy)hydroxyphosphorylamino)-pentanedioic acid
Homo sapiens
-
-
0.00000068
S-2-((2-(S-4-amino-4-carboxybutanamido)-S-2-carboxyethoxy)-hydroxyphosphorylamino)-pentanedioic acid
Homo sapiens
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
activity in prostate tissue homogenate in comparison to other species, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
activity assay
5
-
second optimum at pH 8
7.7
-
assay at, recombinant enzyme
8
-
second optimum at pH 5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
activity assay
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the enzyme is present in human blood, and its concentration within a healthy population varies between 1.3 and 17.2 ng/ml
Manually annotated by BRENDA team
prostate gland
Manually annotated by BRENDA team
considerably increased in prostate carcinoma
Manually annotated by BRENDA team
-
quantitative expression analysis
Manually annotated by BRENDA team
-
ventricular, lumbar, and subarachnoid
Manually annotated by BRENDA team
-
primary cancer
Manually annotated by BRENDA team
-
PSMA is expressed in the neovasculature of multiple nonprostatic solid tumors, it shows a unique expression pattern limited to tumor-associated endothelial cells. Expression in liver metastasis from colorectal cancers and lymph node metastasis from colorectal cancers
Manually annotated by BRENDA team
-
very low enzyme expression level
Manually annotated by BRENDA team
-
prostate cancer cell line
Manually annotated by BRENDA team
-
high expression level
Manually annotated by BRENDA team
-
modeling
Manually annotated by BRENDA team
-
higher level in patients with prostrate cancer, lower levels in healthy male donors
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
associated with
Manually annotated by BRENDA team
additional information
-
Vinca alkaloids destabilize the microtubules leading to basolateral expression of the enzyme and its integration into the basolateral membrane
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
the enzyme is involved in neurological disorders and overexpressed in a number of solid cancers
metabolism
acute exposure to valproic acid, a drug used for bipolar disorder and epilepsy and a known histone deacetylase inhibitor, for 4-6 h increases the glutamate carboxypeptidase II protein level in human astrocyte U-87MG cells but does not have a similar effect after 12-24 h exposure. Valproic acid does not affect the glutamate carboxypeptidase II mRNA expression, but decrease in glutamate carboxypeptidase II protein level by cycloheximide treatment is blocked by valproic acid. The valproic acid-induced increase of glutamate carboxypeptidase II protein level may be dependent on the ubiquitin/proteasome pathway. Valproic acid increases the acetylation of glutamate carboxypeptidase II protein at the lysine residues and facilitates a decrease of the poly-ubiquitinated glutamate carboxypeptidase II level. Similarly, M344, a specific histone deacetylase 1/6 inhibitor, also increases the glutamate carboxypeptidase II protein level
physiological function
malfunction
-
inhibition of the GCP II-catalyzed reaction is beneficial for the treatment of degenerative diseases associated with excess glutamate. Inhibition of GCP II is neuroprotective in a variety of cell and animal models of disease involving excess glutamate. N-acetyl-aspartyl-glutamate can acts as a marker of glutamate carboxypeptidase II inhibition
physiological function
-
PSMA acts as a glutamate-preferring carboxypeptidase in human prostate tissue, and plays a role in folic acid utilization and metabolism
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FOLH1_HUMAN
750
1
84331
Swiss-Prot
Secretory Pathway (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
-
about
84000
-
calculation from sequence of cDNA, short intracellular domain, single transmembrane element, large glubular extracellular domain
additional information
-
domain structure, sequence alignment with transferrin receptor, the catalytic domain can be assigned to the peptidase family M28
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer, the enzyme folds into three domains: a protease-like, an apical, and a C-terminal domain which are all involved in substrate binding, three-dimensional structure analysis, crystal structure
?
-
x * 110000-120000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
treatment with valproic acid increases the acetylation of glutamate carboxypeptidase II protein at the lysine residues and facilitates a decrease of the poly-ubiquitinated glutamate carboxypeptidase II level. Similarly, M344, a specific histone deacetylase 1/6 inhibitor, also increases the glutamate carboxypeptidase II protein level
glycoprotein
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor-diffusion method, crystal structures of human glutamate carboxypeptidase II in complex with a series of phosphoramidate-based inhibitors harboring effector functions of diverse physicochemical characteristics
in complex with inhibitors N-2-([(1S)-1-carboxy-2-(furan-2-yl)ethyl]carbamoyl)-N-6-(4-iodobenzoyl)-L-lysine, N-2-([(1S)-1-carboxybut-3-yn-1-yl]carbamoyl)-N-6-(4-iodobenzoyl)-L-lysine, and N-([(1S)-1-carboxy-5-([(4-iodophenyl)carbonyl]amino)pentyl]carbamoyl)-L-glutamic acid, PDB entries 4OC2, 4OC3, and 3D7H, respectively
purified recombinant extracellular portion of the enzyme, comprising residues 44-750, in complex with GPI-18431, a iodobenzyl derivative of inhibitor 2-PMPA, hanging drop vapour diffusion method, room temperature, 0.002 ml protein solution, containing 0.2 mM GPI-18431, is mixed with 0.002 ml well solution containing 20 mM HEPES, pH 7.5, 0.2 M NaCl, 5% w/v PEG 400, and 15%w/v PEG 1500, 1-2 weeks, X-ray diffraction structure determination and analysis at 2.2 A resolution
purified recombinant His6-tagged extracellular portion, which contains bound Zn2+, hanging drop vapour diffusion method, 0.0008 ml of 10 mg/ml protein in 20 mM Tris, pH 7.5, is mixed with an equal volume of reservoir solution containing 18% PEG 3350, 0.2 M sodium thiocyanate, 4°C, cryoprotection by 20% glycerol, X-ray diffrcation structure determination and analysis at 3.5 A resolution
the crystal structure of GCPII(E424A) in complex with N-acetyl-L-aspartyl-L-glutamate is determined at 1.70 A resolution
the structures of human GCPII in complex with (S)-2-(3-((R)-1-carboxy-(2-methylthio)ethyl)ureido)pentanedioic acid, (S)-2-(3-((S)-1-carboxy-2-(4-hydroxy-3-iodophenyl)ethyl)ureido)pentanedioic acid, (S)-2-(3-((R)-1-carboxy-2-(4-fluorobenzylthio)ethyl)ureido)pentanedioic acid and (S)-2-(3-((S)-1-carboxy-(4-iodobenzamido)pentyl)ureido)pentanedioic acid are solved to a resolution of 1.75, 1.54, 1.69 and 1.55 A, respectively
X-ray crystal structure of glutamate carboxypeptidase II in complex with (S)-2-(3-((S)-1-carboxy-5-(1,2-dicarba-closo-dodecarboranylamido) pentyl)ureido)pentanedioic acid at 1.79 A resolution. The X-ray analysis reveals that the bulky closo-carborane cluster is located in the spacious entrance funnel region of the enzyme, indicating that the carborane cluster can be further structurally modified to identify promising lead structures of novel glutamate carboxypeptidase II inhibitors
X-ray structure of human glutamate carboxypeptidase II in complex with hydroxamate-based inhibitors
X-ray structure of the inactive enzyme with the engineered mutation E424A in complex with beta-citrylglutamate, hanging drop vapour diffusion method
X-ray structures of seven complexes of the hydrolytically inactive recombinant E424A mutant and polyglutamylated folates substrates, refined at resolutions of between 1.65 and 2.00 A, and mutant H475Y, in complex with substrate N-acetyl-L-aspartyl-L-glutamate to 1.83 A resolution
GCPIII ectodomain in a pseudo-unliganded state and in a complex with product L-glutamate, or the phosphapeptide transition state mimetic (2S,3'S)-[[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl]-pentanedioic acid, or quisqualic acid, a glutamate biostere, X-ray diffraction structure determination and analysis at 1.29-1.56 A resolution, modelling
-
prostate-specific membrane antigen crystal structure analysis
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E424A
H475Y
X-ray structure in complex with substrate N-acetyl-L-aspartyl-L-glutamate,wild-type and the H475 variant are functionally identical. both proteins share an almost identical arrangement of amino acids in the vicinity of residue 475, and the imidazole ring of wild-type His475 and the benzene ring of Tyr475 overlap spatiallyl
K479R
in the presence of cycloheximide the mutant is less ubiquitinylated and degraded. Decrease in the level of glutamate carboxypeptidase II protein by histone deacetylase is significantly blocked by K479R mutants
K491R
in the presence of cycloheximide the mutant is less ubiquitinylated and degraded
R463L
no major differences between the mutant and the wild-type enzyme for the kinetic parameters of folyl-gamma-L-glutamic acid hydrolysis, a slight decrease in KM values for both N-acetyl-L-aspartyl-L-glutamate and folyl-(gamma-L-glutamic acid)2, folyl-(gamma-L-glutamic acid)3, folyl-(gamma-L-glutamic acid)4
R511L
no major differences between the mutant and the wild-type enzyme for the kinetic parameters of folyl-gamma-L-glutamic acid hydrolysis, a slight decrease in KM values for both N-acetyl-L-aspartyl-L-glutamate and folyl-(gamma-L-glutamic acid)2, folyl-(gamma-L-glutamic acid)3, folyl-(gamma-L-glutamic acid)4
W541A
no major differences between the mutant and the wild-type enzyme for the kinetic parameters of folyl-gamma-L-glutamic acid hydrolysis, a slight decrease in KM values for both N-acetyl-L-aspartyl-L-glutamate and folyl-(gamma-L-glutamic acid)2, folyl-(gamma-L-glutamic acid)3, folyl-(gamma-L-glutamic acid)4
DELTA1-42
-
the recombinantly expressed extracellular domain has a cytosolic localization compared to sell surface membrane localization of the full-length enzyme. Less than 5% of the activity of the wild-type enzyme
DELTA20-42
-
mutant enzyme omitting the transmembrane domain is associated with the cell surface membrane as is the full-length enzyme. Less than 5% of the activity of the wild-type enzyme
H380G
-
site-directed mutagenesis, active site mutant, inactive mutant
H475Y
-
C1561T single nucleotide polymorphism located in the putative catalytic region of the enzyme
L4A/L5A
-
site-directed mutagenesis, internalization motif mutant, active mutant, no endocytic internalization
N121A
-
site-directed mutagenesis of an N-glycosylation site, nearly inactive enzyme
N140A
-
site-directed mutagenesis of an N-glycosylation site, nearly inactive enzyme
N153A
-
site-directed mutagenesis of an N-glycosylation site, nearly inactive enzyme
N195A
-
site-directed mutagenesis of an N-glycosylation site, nearly inactive enzyme
N336A
N459A
-
site-directed mutagenesis, glycosylation site E mutant, inactive mutant, no endocytic internalization
N476A
N51A
-
site-directed mutagenesis of an N-glycosylation site leads to 75% reduced activity compared to the wild-type enzyme
N638A
N76A
-
site-directed mutagenesis of an N-glycosylation site leads to 25% reduced activity compared to the wild-type enzyme
T640A
-
site-directed mutagenesis of an N-glycosylation site, nearly inactive enzyme
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
acetylation of glutamate carboxypeptidase II is facilitated by histone deacetylase 1, and the acetylated glutamate carboxypeptidase II is more stable than the non-acetylated glutamate carboxypeptidase II. The stability of the carboxypeptidase II protein is regulated by histone deacetylase 1 through acetylation at the lysine 479 residue
even a slight disruption of the Ca2+-binding site destabilizes the three-dimensional fold of the enzyme
stability of glutamate carboxypeptidase II protein is regulated by histone deacetylases 1 through acetylation at the lysine 479 residue.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
efficient one-step purification method yields purified recombinant enzyme
purification consists of four steps, QAE-Sephadex A50 batch chromatography, chromatography on a Source 15S column, affinity chromatography using lentil lectin Sepharose, and gel filtration on a Superdex 200 column
recombinant His6-tagged extracellular portion of the enzyme from High5 by nickel affinity chromatography and gel filtration
FLAG affinity chromatography, full-length enzyme and mutant enzymes DELTA1-42 and DELTA20-42
-
native enzyme from LNCaP cells by conformational epitope-specific antibody-affinity chromatography in presence of Zn2+ in a native and active conformation
-
partially by membrane preparation
-
recombinant enzyme from CHO cells partially by membrane preparation
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning and expression of the His6-tagged extracellular portion of the enzyme in High5 cells using the baculovirus transfection system, secretion of the glycosylated extracellular domain
expression in Drosophila S2 cells
expression in PC3 cell
for expression in Drosophila Schneiders S2 cells
genetic structure, overview
the extracellular part, amino acids 44-750, of human GCPII is cloned and heterologously overexpressed in Drosophila Schneiders S2 cells
construction of the DNA vaccines carrying truncated human tPSMA gene driven by the cytomegalovirus promoter and mouse 4-1BBL gene driven by an IRES
-
expression in CHO cells
-
expression in COS-1 cells, mannose-rich glycosylation of the recombinant enzyme in absence of an inhibitor, recombinant glycosylation and subcellular transport analysis, overview, stable expression in MDCK cells at the cell surface
-
expression in DU145 cell line
-
expression of the full-length enzyme and the mutant enzymes DEALTA20-42 and DELTA1-42 in HEK293 cells
-
expression of wild-type and mutant enzymes in PC3 cells
-
gene FOLH1, DNA sequence variants analysis, expression regulation by PMSA enhancer, PSME, involving Ca2+, overview, localization on chromosome 11p11-12, another highly homologous gene is located at 11q14.3 and is expressed in several tissues, e.g. kidney and liver, but not in prostate
-
stable expression in MDCK cells of truncated PMSA-DELTA103-750 as GFP-fusion protein and of the extracellular domain
-
stable expression of wild-type and mutant enzymes in S2 cells, secretion of the enzyme, which is prevented by blocking the N-glycosylation
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Lentivirus-mediated RNAi inhibits PSMA mRNA and protein expression in LNCaP and DU-145 cells, PSMA RNAi induces the changes of cell cycle, overview
androgen ablation can up-regulate PSMA expression
-
docetaxel down-regulates the expression of androgen receptor and prostate-specific antigen but not prostate-specific membrane antigen in prostate cancer cell lines
-
inhibition of LNCaP cell growth by mono- and bispecific antisense oligonucleotides directed against bcl-2 and epidermal growth factor receptor, EGFR, inhibition of expression of non-targeted proteins prostate-specific membrane antigen only by bcl-2-monospecific oligos, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
synthesis of a series of PSMA-targeted 99mTc-chelate complexes, with core ligand 2-[3-(3-benzyloxycarbonyl-1-tert-butoxycarbonyl-propyl)-ureido]pentanedioic acid di-tert-butyl ester, for imaging PSMA-expressing human prostate cancer cells, in silico docking studies using the crystal structure of PSMA, overview. The method offers a potential for use in localizing prostate cancer masses, monitoring response to therapy, detecting prostate cancer recurrence following surgery, and selecting patients for subsequent PSMAtargeted chemotherapy
diagnostics
medicine
pharmacology
the enzyme is a drug target in neuronal damage and prostate cancer
diagnostics
drug development
-
PSMA is a target for drug design
medicine
pharmacology
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rawlings, N.D.; Barrett, A.J.
Structure of membrane glutamate carboxypeptidase
Biochim. Biophys. Acta
1339
247-252
1997
Homo sapiens
Manually annotated by BRENDA team
Gregorakis, A.K.; Holmes, E.H.; Murphy, G.P.
Prostrate-specific membrane antigen: current and future utility
Semin. Urol. Oncol.
16
2-12
1998
Homo sapiens
Manually annotated by BRENDA team
Maraj, B.H.; Whelan, P.; Markham, A.F.
Prostate-specific membrane antigen
Br. J. Urol.
81
523-528
1998
Homo sapiens
Manually annotated by BRENDA team
Fair, W.R.; Israeli, R.S.; Heston, W.D.W.
Prostrate-specific membrane antigen
Prostate
32
140-148
1997
Homo sapiens
Manually annotated by BRENDA team
Carter, R.E.; Feldman, A.R.; Coyle, J.T.
Prostrate-specific membrane antigen is a hydrolase with substrate and pharmacologic characteristics of a neuropeptidase
Proc. Natl. Acad. Sci. USA
93
749-753
1996
Homo sapiens
Manually annotated by BRENDA team
Pinto, J.T.; Suffoletto, B.P.; Berzin, T.M.; Qiao, C.H.; Lin, S.; Tong, W.P.; May, F.; Mukherjee, B.; Heston, W.D.W.
Prostate-specific membrane antigen: a novel folate hydrolase in human prostatic carcinoma cells
Clin. Cancer Res.
2
1445-1451
1996
Homo sapiens
Manually annotated by BRENDA team
Heston, W.D.W.
Characterization and glutamyl preferring carboxypeptidase function of prostrate specific membrane antigen: a novel folate hydrolase
Urology
49 (3A Suppl)
104-112
1997
Homo sapiens
Manually annotated by BRENDA team
Troyer, J.K.; Beckett, M.L.; Wright, G.L.
Location of prostrate-specific membrane antigen in the LNCaP prostrate carcinoma cell line
Prostate
30
232-242
1997
Homo sapiens
Manually annotated by BRENDA team
Rojas, C.; Frazier, S.T.; Flanary, J.; Slusher, B.S.
Kinetics and inhibition of glutamate carboxypeptidase II using a microplate assay
Anal. Biochem.
310
50-54
2002
Homo sapiens
Manually annotated by BRENDA team
Rodriguez, C.E.; Lu, H.; Martinez, A.R.; Hu, Y.; Brunelle, A.; Berkman, C.E.
Inhibition of glutamate carboxypeptidase II by phosphonamidothionate derivatives of glutamic acid
J. Enzyme Inhib.
16
359-365
2001
Homo sapiens
Manually annotated by BRENDA team
Kozikowski, A.P.; Zhang, J.; Nan, F.; Petukhov, P.A.; Grajkowska, E.; Wroblewski, J.T.; Yamamoto, T.; Bzdega, T.; Wroblewska, B.; Neale, J.H.
Synthesis of urea-based inhibitors as active site probes of glutamate carboxypeptidase II: efficacy as analgesic agents
J. Med. Chem.
47
1729-1738
2004
Homo sapiens
Manually annotated by BRENDA team
Meighan, M.A.; Dickerson, M.T.; Glinskii, O.; Glinsky, V.V.; Wright, G.L., Jr.; Deutscher, S.L.
Recombinant glutamate carboxypeptidase II (prostate specific membrane antigen-PSMA)-cellular localization and bioactivity analyses
J. Protein Chem.
22
317-326
2003
Homo sapiens
Manually annotated by BRENDA team
Thomas, A.G.; Wozniak, K.M.; Tsukamoto, T.; Calvin, D.; Wu, Y.; Rojas, C.; Vornov, J.; Slusher, B.S.
Glutamate carboxypeptidase II (NAALADase) inhibition as a novel therapeutic strategy
Adv. Exp. Med. Biol.
576
327-37
2006
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
van der Post, J.P.; de Visser, S.J.; de Kam, M.L.; Woelfler, M.; Hilt, D.C.; Vornov, J.; Burak, E.S.; Bortey, E.; Slusher, B.S.; Limsakun, T.; Cohen, A.F.; van Gerven, J.M.
The central nervous system effects, pharmacokinetics and safety of the NAALADase-inhibitor GPI 5693
Br. J. Clin. Pharmacol.
60
128-136
2005
Homo sapiens
Manually annotated by BRENDA team
Ghosh, A.; Wang, X.; Klein, E.; Heston, W.D.
Novel role of prostate-specific membrane antigen in suppressing prostate cancer invasiveness
Cancer Res.
65
727-731
2005
Homo sapiens
Manually annotated by BRENDA team
Mesters, J.R.; Barinka, C.; Li, W.; Tsukamoto, T.; Majer, P.; Slusher, B.S.; Konvalinka, J.; Hilgenfeld, R.
Structure of glutamate carboxypeptidase II, a drug target in neuronal damage and prostate cancer
EMBO J.
25
1375-1384
2006
Homo sapiens (Q04609)
Manually annotated by BRENDA team
Yamamoto, T.; Hirasawa, S.; Wroblewska, B.; Grajkowska, E.; Zhou, J.; Kozikowski, A.; Wroblewski, J.; Neale, J.H.
Antinociceptive effects of N-acetylaspartylglutamate (NAAG) peptidase inhibitors ZJ-11, ZJ-17 and ZJ-43 in the rat formalin test and in the rat neuropathic pain model
Eur. J. Neurosci.
20
483-494
2004
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Marchal, C.; Redondo, M.; Padilla, M.; Caballero, J.; Rodrigo, I.; Garcia, J.; Quian, J.; Boswick, D.G.
Expression of prostate specific membrane antigen (PSMA) in prostatic adenocarcinoma and prostatic intraepithelial neoplasia
Histol. Histopathol.
19
715-718
2004
Homo sapiens
Manually annotated by BRENDA team
Castelletti, D.; Fracasso, G.; Alfalah, M.; Cingarlini, S.; Colombatti, M.; Naim, H.Y.
Apical transport and folding of prostate-specific membrane antigen occurs independent of glycan processing
J. Biol. Chem.
281
3505-3512
2006
Homo sapiens
Manually annotated by BRENDA team
Ghosh, A.; Heston, W.D.
Tumor target prostate specific membrane antigen (PSMA) and its regulation in prostate cancer
J. Cell. Biochem.
91
528-539
2004
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Tsukamoto, T.; Majer, P.; Vitharana, D.; Ni, C.; Hin, B.; Lu, X.C.; Thomas, A.G.; Wozniak, K.M.; Calvin, D.C.; Wu, Y.; Slusher, B.S.; Scarpetti, D.; Bonneville, G.W.
Enantiospecificity of glutamate carboxypeptidase II inhibition
J. Med. Chem.
48
2319-2324
2005
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Majer, P.; Hin, B.; Stoermer, D.; Adams, J.; Xu, W.; Duvall, B.R.; Delahanty, G.; Liu, Q.; Stathis, M.J.; Wozniak, K.M.; Slusher, B.S.; Tsukamoto, T.
Structural optimization of thiol-based inhibitors of glutamate carboxypeptidase II by modification of the P1 side chain
J. Med. Chem.
49
2876-2885
2006
Homo sapiens
Manually annotated by BRENDA team
Christiansen, J.J.; Rajasekaran, S.A.; Inge, L.; Cheng, L.; Anilkumar, G.; Bander, N.H.; Rajasekaran, A.K.
N-glycosylation and microtubule integrity are involved in apical targeting of prostate-specific membrane antigen: implications for immunotherapy
Mol. Cancer Ther.
4
704-714
2005
Homo sapiens
Manually annotated by BRENDA team
Zhou, J.; Neale, J.H.; Pomper, M.G.; Kozikowski, A.P.
NAAG peptidase inhibitors and their potential for diagnosis and therapy
Nat. Rev. Drug Discov.
4
1015-1026
2005
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Ghose, S.; Weickert, C.S.; Colvin, S.M.; Coyle, J.T.; Herman, M.M.; Hyde, T.M.; Kleinman, J.E.
Glutamate carboxypeptidase II gene expression in the human frontal and temporal lobe in schizophrenia
Neuropsychopharmacology
29
117-125
2004
Homo sapiens
Manually annotated by BRENDA team
Davis, M.I.; Bennett, M.J.; Thomas, L.M.; Bjorkman, P.J.
Crystal structure of prostate-specific membrane antigen, a tumor marker and peptidase
Proc. Natl. Acad. Sci. USA
102
5981-5986
2005
Homo sapiens (Q04609)
Manually annotated by BRENDA team
Aggarwal, S.; Ricklis, R.M.; Williams, S.A.; Denmeade, S.R.
Comparative study of PSMA expression in the prostate of mouse, dog, monkey, and human
Prostate
66
903-910
2006
Canis lupus familiaris, Macaca fascicularis, Homo sapiens, Macaca mulatta, Mus musculus
Manually annotated by BRENDA team
Liu, T.; Toriyabe, Y.; Berkman, C.E.
Purification of prostate-specific membrane antigen using conformational epitope-specific antibody-affinity chromatography
Protein Expr. Purif.
49
251-255
2006
Homo sapiens
Manually annotated by BRENDA team
Barinka, C.; Sacha, P.; Sklenar, J.; Man, P.; Bezouska, K.; Slusher, B.S.; Konvalinka, J.
Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity
Protein Sci.
13
1627-1635
2004
Homo sapiens
Manually annotated by BRENDA team
Ding, P.; Helquist, P.; Miller, M.J.
Design, synthesis and pharmacological activity of novel enantiomerically pure phosphonic acid-based NAALADase inhibitors
Org. Biomol. Chem.
5
826-831
2007
Homo sapiens
Manually annotated by BRENDA team
Klusak, V.; Barinka, C.; Plechanovova, A.; Mlcochova, P.; Konvalinka, J.; Rulisek, L.; Lubkowski, J.
Reaction mechanism of glutamate carboxypeptidase II revealed by mutagenesis, X-ray crystallography, and computational methods
Biochemistry
48
4126-4138
2009
Homo sapiens (Q04609), Homo sapiens
Manually annotated by BRENDA team
Lopreato, F.R.; Stabler, S.P.; Carvalho, F.R.; Hirata, R.D.; Hirata, M.H.; Robi, D.L.; Sampaio-Neto, L.F.; Allen, R.H.; Guerra-Shinohara, E.M.
Relationships between gene polymorphisms of folate-related proteins and vitamins and metabolites in pregnant women and neonates
Clin. Chim. Acta
398
134-139
2008
Homo sapiens
Manually annotated by BRENDA team
Barinka, C.; Byun, Y.; Dusich, C.L.; Banerjee, S.R.; Chen, Y.; Castanares, M.; Kozikowski, A.P.; Mease, R.C.; Pomper, M.G.; Lubkowski, J.
Interactions between human glutamate carboxypeptidase II and urea-based inhibitors: structural characterization
J. Med. Chem.
51
7737-7743
2008
Homo sapiens (Q04609), Homo sapiens
Manually annotated by BRENDA team
Guilarte, T.R.; Hammoud, D.A.; McGlothan, J.L.; Caffo, B.S.; Foss, C.A.; Kozikowski, A.P.; Pomper, M.G.
Dysregulation of glutamate carboxypeptidase II in psychiatric disease
Schizophr. Res.
99
324-332
2008
Homo sapiens
Manually annotated by BRENDA team
Thomas, A.G.; Rojas, C.J.; Hill, J.R.; Shaw, M.; Slusher, B.S.
Bioanalysis of N-acetyl-aspartyl-glutamate as a marker of glutamate carboxypeptidase II inhibition
Anal. Biochem.
404
94-96
2010
Homo sapiens
Manually annotated by BRENDA team
Liu, T.; Wu, L.Y.; Berkman, C.E.
Prostate-specific membrane antigen-targeted photodynamic therapy induces rapid cytoskeletal disruption
Cancer Lett.
296
106-112
2010
Homo sapiens
Manually annotated by BRENDA team
Hillier, S.M.; Maresca, K.P.; Femia, F.J.; Marquis, J.C.; Foss, C.A.; Nguyen, N.; Zimmerman, C.N.; Barrett, J.A.; Eckelman, W.C.; Pomper, M.G.; Joyal, J.L.; Babich, J.W.
Preclinical evaluation of novel glutamate-urea-lysine analogues that target prostate-specific membrane antigen as molecular imaging pharmaceuticals for prostate cancer
Cancer Res.
69
6932-6940
2009
Homo sapiens
Manually annotated by BRENDA team
Regino, C.A.; Wong, K.J.; Milenic, D.E.; Holmes, E.H.; Garmestani, K.; Choyke, P.L.; Brechbiel, M.W.
Preclinical evaluation of a monoclonal antibody (3C6) specific for prostate-specific membrane antigen
Curr. Radiopharm.
2
9-17
2009
Homo sapiens
Manually annotated by BRENDA team
Dharmasiri, U.; Balamurugan, S.; Adams, A.A.; Okagbare, P.I.; Obubuafo, A.; Soper, S.A.
Highly efficient capture and enumeration of low abundance prostate cancer cells using prostate-specific membrane antigen aptamers immobilized to a polymeric microfluidic device
Electrophoresis
30
3289-3300
2009
Homo sapiens
Manually annotated by BRENDA team
Hlouchova, K.; Barinka, C.; Konvalinka, J.; Lubkowski, J.
Structural insight into the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III
FEBS J.
276
4448-4462
2009
Homo sapiens
Manually annotated by BRENDA team
Haffner, M.C.; Kronberger, I.E.; Ross, J.S.; Sheehan, C.E.; Zitt, M.; Muehlmann, G.; Ofner, D.; Zelger, B.; Ensinger, C.; Yang, X.J.; Geley, S.; Margreiter, R.; Bander, N.H.
Prostate-specific membrane antigen expression in the neovasculature of gastric and colorectal cancers
Hum. Pathol.
40
1754-1761
2009
Homo sapiens
Manually annotated by BRENDA team
Maresca, K.; Hillier, S.; Femia, F.; Keith, D.; Barone, C.; Joyal, J.; Zimmerman, C.; Kozikowski, A.; Barrett, J.; Eckelman, W.; Babich, J.
A series of halogenated heterodimeric inhibitors of prostate specific membrane antigen (PSMA) as radiolabeled probes for targeting prostate cancer
J. Med. Chem.
52
347-357
2009
Homo sapiens
Manually annotated by BRENDA team
Lapi, S.E.; Wahnishe, H.; Pham, D.; Wu, L.Y.; Nedrow-Byers, J.R.; Liu, T.; Vejdani, K.; VanBrocklin, H.F.; Berkman, C.E.; Jones, E.F.
Assessment of an 18F-labeled phosphoramidate peptidomimetic as a new prostate-specific membrane antigen-targeted imaging agent for prostate cancer
J. Nucl. Med.
50
2042-2048
2009
Homo sapiens
Manually annotated by BRENDA team
Elsaesser-Beile, U.; Reischl, G.; Wiehr, S.; Buehler, P.; Wolf, P.; Alt, K.; Shively, J.; Judenhofer, M.S.; Machulla, H.J.; Pichler, B.J.
PET imaging of prostate cancer xenografts with a highly specific antibody against the prostate-specific membrane antigen
J. Nucl. Med.
50
606-611
2009
Homo sapiens
Manually annotated by BRENDA team
Rubenstein, M.; Hollowell, C.M.; Guinan, P.
Increased prostate-specific membrane antigen expression in LNCaP cells following treatment with bispecific antisense oligonucleotides directed against bcl-2 and EGFR
Med. Oncol.
27
1212-1218
2009
Homo sapiens
Manually annotated by BRENDA team
Guo, Z.; Huang, H.; Zeng, L.; Du, T.; Xu, K.; Lin,T.; Jiang, C.; Dong, W.; Cao, Y.; Chen, J.; Zhong, W.; Huang, J.
Lentivirus-mediated RNAi knockdown of prostate-specific membrane antigen suppresses growth, reduces migration ability and the invasiveness of prostate cancer cells
Med. Oncol.
28
878-887
2011
Homo sapiens (Q04609)
Manually annotated by BRENDA team
Kularatne, S.A.; Wang, K.; Santhapuram, H.K.; Low, P.S.
Prostate-specific membrane antigen targeted imaging and therapy of prostate cancer using a PSMA inhibitor as a homing ligand
Mol. Pharm.
6
780-789
2009
Homo sapiens (Q04609), Homo sapiens
Manually annotated by BRENDA team
Kularatne, S.A.; Zhou, Z.; Yang, J.; Post, C.B.; Low, P.S.
Design, synthesis, and preclinical evaluation of prostate-specific membrane antigen targeted (99m)Tc-radioimaging agents
Mol. Pharm.
6
790-800
2009
Homo sapiens
Manually annotated by BRENDA team
Mannweiler, S.; Amersdorfer, P.; Trajanoski, S.; Terrett, J.; King, D.; Mehes, G.
Heterogeneity of prostate-specific membrane antigen (PSMA) expression in prostate carcinoma with distant metastasis
Pathol. Oncol. Res.
15
167-172
2009
Homo sapiens
Manually annotated by BRENDA team
Colombatti, M.; Grasso, S.; Porzia, A.; Fracasso, G.; Scupoli, M.T.; Cingarlini, S.; Poffe, O.; Naim, H.Y.; Heine, M.; Tridente, G.; Mainiero, F.; Ramarli, D.
The prostate specific membrane antigen regulates the expression of IL-6 and CCL5 in prostate tumour cells by activating the MAPK pathways
PLoS ONE
4
e4608
2009
Homo sapiens
Manually annotated by BRENDA team
Ananias, H.J.; van den Heuvel, M.C.; Helfrich, W.; de Jong, I.J.
Expression of the gastrin-releasing peptide receptor, the prostate stem cell antigen and the prostate-specific membrane antigen in lymph node and bone metastases of prostate cancer
Prostate
69
1101-1108
2009
Homo sapiens
Manually annotated by BRENDA team
Liu, C.; Hasegawa, K.; Russell, S.J.; Sadelain, M.; Peng, K.W.
Prostate-specific membrane antigen retargeted measles virotherapy for the treatment of prostate cancer
Prostate
69
1128-1141
2009
Homo sapiens
Manually annotated by BRENDA team
Kuroda, K.; Liu, H.; Kim, S.; Guo, M.; Navarro, V.; Bander, N.H.
Docetaxel down-regulates the expression of androgen receptor and prostate-specific antigen but not prostate-specific membrane antigen in prostate cancer cell lines: implications for PSA surrogacy
Prostate
69
1579-1585
2009
Homo sapiens
Manually annotated by BRENDA team
Liu, T.; Wu, L.Y.; Choi, J.K.; Berkman, C.E.
In vitro targeted photodynamic therapy with a pyropheophorbide - a conjugated inhibitor of prostate-specific membrane antigen
Prostate
69
585-594
2009
Homo sapiens
Manually annotated by BRENDA team
Kuang, Y.; Zhu, H.; Weng, X.; Liu, X.; Chen, Z.; Chen, H.; Jiang, B.; Zheng, Y.
Antitumor immune response induced by DNA vaccine encoding human prostate-specific membrane antigen and mouse 4-1BBL
Urology
76
510e1-510e6
2010
Homo sapiens
Manually annotated by BRENDA team
Lee, S.; Kim, H.; Cheong, Y.; Kim, M.; Jo, S.; Youn, H.; Park, S.
S1 pocket of glutamate carboxypeptidase II: A new binding site for amyloid-beta degradation
Biochem. Biophys. Res. Commun.
438
765-771
2013
Homo sapiens (Q04609)
Manually annotated by BRENDA team
Choi, J.; Kim, J.; Jo, S.
Acetylation regulates the stability of glutamate carboxypeptidase II protein in human astrocytes
Biochem. Biophys. Res. Commun.
450
372-377
2014
Homo sapiens (Q04609), Homo sapiens
Manually annotated by BRENDA team
Pavlicek, J.; Ptacek, J.; Cerny, J.; Byun, Y.; Skultetyova, L.; Pomper, M.G.; Lubkowski, J.; Barinka, C.
Structural characterization of P1-diversified urea-based inhibitors of glutamate carboxypeptidase II
Bioorg. Med. Chem. Lett.
24
2340-2345
2014
Homo sapiens (Q04609), Homo sapiens
Manually annotated by BRENDA team
Alt, J.; Stathis, M.; Rojas, C.; Slusher, B.
Glutamate carboxypeptidase II is not an amyloid peptide-degrading enzyme
FASEB J.
27
2620-2625
2013
Homo sapiens (Q04609), Homo sapiens
Manually annotated by BRENDA team
Navratil, M.; Ptacek, J.; Sacha, P.; Starkova, J.; Lubkowski, J.; Bakinka, C.; Konvalinka, J.
Structural and biochemical characterization of the folyl-poly-gamma-L-glutamate hydrolyzing activity of human glutamate carboxypeptidase II
FEBS J.
281
3228-3242
2014
Homo sapiens (Q04609), Homo sapiens
Manually annotated by BRENDA team
Knedlik, T.; Navratil, V.; Vik, V.; Pacik, D.; Sacha, P.; Konvalinka, J.
Detection and quantitation of glutamate carboxypeptidase II in human blood
Prostate
74
768-780
2014
Homo sapiens (Q04609), Homo sapiens
Manually annotated by BRENDA team
Lee, S.K.; Kim, H.; Cheong, Y.H.; Kim, M.J.; Jo, S.A.; Youn, H.S.; Park, S.I.
S1 pocket of glutamate carboxypeptidase II a new binding site for amyloid-beta degradation
Biochem. Biophys. Res. Commun.
438
765-771
2013
Homo sapiens (Q04609)
Manually annotated by BRENDA team
Choi, J.-Y.; Kim, J.-H.; Jo, S.A.
Acetylation regulates the stability of glutamate carboxypeptidase II protein in human astrocytes
Biochem. Biophys. Res. Commun.
450
372-377
2014
Homo sapiens (Q04609), Homo sapiens
Manually annotated by BRENDA team
Choi, J.Y.; Ko, J.H.; Jo, S.A.
HDAC1 regulates the stability of glutamate carboxypeptidase II protein by modulating acetylation status of lysine 479 residue
Biochem. Biophys. Res. Commun.
497
416-423
2018
Homo sapiens (Q04609), Homo sapiens
Manually annotated by BRENDA team
Youn, S.; Kim, K.; Ptacek, J.; Ok, K.; Novakova, Z.; Kim, Y.; Koo, J.; Barinka, C.; Byun, Y.
Carborane-containing urea-based inhibitors of glutamate carboxypeptidase II Synthesis and structural characterization
Bioorg. Med. Chem. Lett.
25
5232-5236
2015
Homo sapiens (Q04609)
Manually annotated by BRENDA team
Novakova, Z.; Cerny, J.; Choy, C.J.; Nedrow, J.R.; Choi, J.K.; Lubkowski, J.; Berkman, C.E.; Barinka, C.
Design of composite inhibitors targeting glutamate carboxypeptidase II the importance of effector functionalities
FEBS J.
283
130-143
2016
Homo sapiens (Q04609), Homo sapiens
Manually annotated by BRENDA team
Navratil, M.; Tykvart, J.; Schimer, J.; Pachl, P.; Navratil, V.; Rokob, T.; Hlouchova, K.; Rulisek, L.; Konvalinka, J.
Comparison of human glutamate carboxypeptidases II and III reveals their divergent substrate specificities
FEBS J.
283
2528-2545
2016
Homo sapiens (Q04609), Homo sapiens
Manually annotated by BRENDA team
Knedlik, T.; Vorlova, B.; Navratil, V.; Tykvart, J.; Sedlak, F.; Vaculin, S.; Franek, M.; Sacha, P.; Konvalinka, J.
Mouse glutamate carboxypeptidase II (GCPII) has a similar enzyme activity and inhibition profile but a different tissue distribution to human GCPII
FEBS Open Bio
7
1362-1378
2017
Mus musculus (O35409), Mus musculus, Homo sapiens (Q04609), Homo sapiens
Manually annotated by BRENDA team
Tykvart, J.; Schimer, J.; Jankarik, A.; Barinkova, J.; Navratil, V.; Starkova, J.; Sramkova, K.; Konvalinka, J.; Majer, P.; Sacha, P.
Design of highly potent urea-based, exosite-binding inhibitors selective for glutamate carboxypeptidase II
J. Med. Chem.
58
4357-4363
2015
Homo sapiens (Q04609), Homo sapiens
Manually annotated by BRENDA team
Novakova, Z.; Wozniak, K.; Jancarik, A.; Rais, R.; Wu, Y.; Pavlicek, J.; Ferraris, D.; Havlinova, B.; Ptacek, J.; Vavra, J.; Hin, N.; Rojas, C.; Majer, P.; Slusher, B.S.; Tsukamoto, T.; Barinka, C.
Unprecedented binding mode of hydroxamate-based inhibitors of glutamate carboxypeptidase II structural characterization and biological activity
J. Med. Chem.
59
4539-4550
2016
Homo sapiens (Q04609), Homo sapiens
Manually annotated by BRENDA team
Naushad, S.M.; Janaki Ramaiah, M.; Stanley, B.A.; Prasanna Lakshmi, S.; Vishnu Priya, J.; Hussain, T.; Alrokayan, S.A.; Kutala, V.K.
In silico approaches to identify the potential inhibitors of glutamate carboxypeptidase II (GCPII) for neuroprotection
J. Theor. Biol.
406
137-142
2016
Homo sapiens (Q04609)
Manually annotated by BRENDA team
Knedlik, T.; Nayvratil, V.; Vik, V.; Pacik, D.; Sacha, P.; Konvalinka, J.
Detection and quantitation of glutamate carboxypeptidase II in human blood
Prostate
74
768-780
2014
Homo sapiens (Q04609), Homo sapiens
Manually annotated by BRENDA team
Ptacek, J.; Nedvedova, J.; Navratil, M.; Havlinova, B.; Konvalinka, J.; Barinka, C.
The calcium-binding site of human glutamate carboxypeptidase II is critical for dimerization, thermal stability, and enzymatic activity
Protein Sci.
27
1575-1584
2018
Homo sapiens (Q04609), Homo sapiens
Manually annotated by BRENDA team