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Information on EC 3.4.17.21 - Glutamate carboxypeptidase II
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3.4.17.21 Glutamate carboxypeptidase IISpecify your search results
Word Map
- 3.4.17.21
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tomography
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positron
- metastases
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psma-targeted
- node
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lncap
-
tracer
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prostatectomy
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castration-resistant
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modal
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radioligands
- androgen
-
psma-positive
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radiotherapy
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radionuclide
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68ga-psma
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biodistribution
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radiotracers
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neovasculature
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radiopharmaceutical
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mcrpc
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theranostic
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pelvic
-
gleason
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psma-expressing
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suvmax
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restaging
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oligometastatic
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68ga-labeled
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multiparametric
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urea-based
-
spect
-
dosimetry
-
scintigraphy
- abiraterone
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castrate-resistant
- n-acetylaspartate
-
extraprostatic
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mpmri
-
pet-ct
-
enzalutamide
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18f-labeled
-
positron-emission
-
tomography-computed
-
radium-223
- pharmacology
-
radioimmunotherapy
- medicine
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tumor-to-background
- analysis
-
radiometals
-
postprostatectomy
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per-patient
- diagnostics
- drug development
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
100 kDa ileum brush border membrane protein
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-
-
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Acetylaspartylglutamate dipeptidase
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-
-
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Dipeptidase, acetylaspartylglutamate
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EC 3.4.19.8
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formerly
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FGCP
folate hydrolase
FOLH1
Folylpoly-gamma-glutamate carboxypeptidase
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-
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GCP II
GCPII
GCPIII
glutamate carboxypeptidase II
glutamate carboxypeptidase III
GPCPII
I100
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-
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Ileal dipeptidylpeptidase
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-
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Membrane glutamate carboxypeptidase
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-
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mGCP
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-
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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
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-
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NAAG peptidase
NAALA dipeptidase
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-
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NAALADase
PMSA
prostate specific membrane antigen
Prostate-specific membrane antigen
Prostate-specific membrane antigen homolog
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-
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Prostrate-specific membrane antigen
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-
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PSM
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-
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PSM antigen
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-
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PSMA
Pteroylpoly-gamma-glutamate carboxypeptidase
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-
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Rat NAAG peptidase
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-
-
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additional information
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glutamate carboxypeptidase III and glutamate carboxypeptidase II belong to the transferrin receptor/glutamate carboxypeptidase II superfamily
FGCP
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-
-
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GCPII
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glutamate carboxypeptidase II
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N-Acetylated alpha-linked acidic dipeptidase
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N-Acetylated alpha-linked acidic dipeptidase
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N-Acetylated-alpha-linked acidic dipeptidase
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N-Acetylated-alpha-linked-acidic dipeptidase
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NAALADase
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NAALADase
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Prostate-specific membrane antigen
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Prostate-specific membrane antigen
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PSMA
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PSMA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates
release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates
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-
-
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release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates
active site structure, substrate binding involving Asp210, and catalytic reaction mechanism involving Glu424 and the Zn2+ ions, the substrate binding cavity involves residues Arg463, Arg534, Arg536, stabilized by Glu457, Asp465, and Ser454
release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates
substrate recognition and induced-fit substrate binding mode, active site structure, catalytic mechanism involving Glu424
release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates
T640 is involved in catalysis, the N-glycosylation status is important for actalytic activity
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
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-
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-
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PATHWAY SOURCE
PATHWAYS
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CAS REGISTRY NUMBER
COMMENTARY
111070-04-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
amyloid-beta + H2O
?
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
-
-
-
?
folyl-(gamma-L-glutamic acid)3 + H2O
folyl-(gamma-L-glutamic acid)2 + L-glutamate
-
-
-
?
folyl-(gamma-L-glutamic acid)4 + H2O
folyl-(gamma-L-glutamic acid)3 + L-glutamate
-
-
-
?
N-acetyl-alpha L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
-
-
-
-
?
N-acetyl-L-aspartyl-L-glutamate
N-acetyl-L-aspartate + L-glutamate
-
-
-
?
poly-gamma-Glutamylfolate + H2O
L-Glu + gamma-glutamylfolate
-
-
removes sequentially gamma-linked glutamates
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
-
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
i.e. NAAG
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
-
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
enantiospecific reaction
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
i.e. NAAG, a neurodipeptide, the enzyme acts as membrane-bound receptor being recycled through clathrin coated pits, expression regulation within cells and involvement in prostate cancer and metastasis, overview
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
supply of the primary excitatory neurotransmitter glutamate, the enzyme is involved in neurological disorders, and neuropathic and inflammatory pain
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
the enzyme is involved in glutamate-mediated neurodegenerative disorders, enzyme inhibition is a mechanism for reduction of excitotoxic glutamate
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
the enzyme is involved in suppressing prostate cancer invasiveness
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
the enzyme is responsible for cleavage of NAAG to yield free glutamate
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
the essential enzyme is involved in prostate cancer, stroke, amyotrophic lateral sclerosis, and neuropathic pain
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
i.e. NAAG
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
i.e. NAAG
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
i.e. NAAG, C-terminal glutamate recognition
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
-
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
i.e. NAAG
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
-
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
i.e. NAAG
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
-
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
i.e. NAAG, a neurodipeptide, the enzyme acts as membrane-bound receptor being recycled through clathrin coated pits, expression regulation within cells in prostate cancer and metastasis, overview
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
the enzyme inactivates the neurotransmitter in the synaptic cleft
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
the enzyme is responsible for glutamate supply, enzyme inhibition decreases the glutamate and increases the N-acetyl-alpha-L-aspartyl-L-glutamate concentration in the brain, which can be a method to treat opioid tolerance and diminish effects of morphine withdrawal, overview
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-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
i.e. NAAG
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
i.e. NAAG
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
the enzyme is responsible for glutamate supply, enzyme inhibition decreases the glutamate and increases the N-acetyl-alpha-L-aspartyl-L-glutamate concentration in the brain, which can be a method to treat opioid tolerance and diminish effects of morphine withdrawal, overview
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-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
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i.e. NAAG
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-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
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enzyme regulation is mediated by glial glutamate and acetylcholine receptors in the nervous tissue
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-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
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i.e. NAAG
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-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
-
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
enantiospecific reaction
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
enzyme inhibition reduces acute neuronal degeneration and astrocyte damage following lateral fluid percussion traumatic brain injury
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
i.e. NAAG, a neurodipeptide, the enzyme acts as membrane-bound receptor being recycled through clathrin coated pits, expression regulation within cells in prostate cancer and metastasis, overview
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
i.e. NAAG, a presynaptically active endogenous neuropeptide which is cleaved by the enzyme in the extracellular space
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
NAAG peptidase inhibitor reduces acute neuronal degeneration and astrocyte damage following lateral fluid percussion TBI in rats
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
supply of the primary excitatory neurotransmitter glutamate
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
the enzyme is involved in glutamate-mediated neurodegenerative disorders, enzyme inhibition is a mechanism for reduction of excitotoxic glutamate
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
i.e. NAAG
-
-
?
N-acetyl-Asp-Glu + H2O
N-acetyl-Asp + Glu
-
the enzyme converts N-acetylaspartylglutamate from a neuroprotectant to a neurotoxin
-
-
?
N-Acetyl-L-Asp-L-Glu + H2O
?
-
functions as a cell surface peptidase, possibly hydrolzing peptides in prostatic fluid
-
-
?
N-Acetyl-L-Asp-L-Glu + H2O
?
-
may play a role in signaling between non-myelinating Schwann cells and peripheral axons
-
-
?
N-Acetyl-L-Asp-L-Glu + H2O
N-Acetyl-L-Asp + L-Glu
-
-
no formation of acetate
?
N-acetyl-L-aspartyl-L-glutamate + H2O
L-glutamate + N-acetyl-L-aspartate
-
-
-
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
L-glutamate + N-acetyl-L-aspartate
-
NAALADase, a neuropeptidase that produces the neurotransmitter glutamate and N-acetyl-Laspartate throught hydrolysis of N-acetyl-L-aspartyl-L-glutamate
-
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
L-glutamate + N-acetyl-L-aspartate
-
-
-
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-Asp + L-Glu
-
-
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
-
-
-
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
-
-
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
-
-
-
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
-
-
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
-
-
-
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
-
-
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
-
-
-
-
?
additional information
?
-
-
hydrolysis of peptide bonds of Asp or Glu to a Glu residue with unsubstituted alpha-carboxyl group. The amide bonds to Glu from the substituted benzoate in folate and methorexate molecules are resistant to hydrolysis
-
-
?
additional information
?
-
-
the enzyme interacts with filamin leading to internalization of PMSA into cells in the perinuclear region, overview
-
-
?
additional information
?
-
-
bifunctional enzyme performing folate hydrolase and N-acetylated alpha-linked acidic dipeptidase, NAALADase, activities
-
-
?
additional information
?
-
-
bifunctional enzyme performing folate hydrolase and N-acetylated alpha-linked acidic dipeptidase, NAALADase, activities
-
-
?
additional information
?
-
-
bifunctional enzyme performing folate hydrolase and N-acetylated alpha-linked acidic dipeptidase, NAALADase, activities
-
-
?
additional information
?
-
-
intestinal absorption of polyglutamyl folates involves cleavage of the glutamate side chain by FGCP
-
-
?
additional information
?
-
-
cross-linking of cell surface PSMA with specific antibodies activates the small GTPases RAS and RAC1 and the MAPKs p38 and ERK1/2 in prostate carcinoma LNCaP cells via NF-kappaB activation, overview. Proliferation of LNCaP cells is inducible by interleukin-6, CCL5 or by cross-linking of PSMA
-
-
?
additional information
?
-
-
PSMA is highly homologous to N-acetylated alpha-linked acidic dipeptidase, NAALADase
-
-
?
additional information
?
-
-
PSMA-targeted photodynamic therapy on cytoskeletal networks in prostate cancer cells results in rapid disruption of microtubules (alpha-/beta-tubulin), microfilaments (actin), and intermediate filaments (cytokeratin 8/18) in the cytoplasm of LNCaP cells. The collapse of cytoplasmic microtubules and the later nuclear translocation of alpha-/beta-tubulin are the most dramatic alternation, overview
-
-
?
additional information
?
-
-
the S1' pocket, the pharmacophore pocket of GCPIII, is shaped by residues Phe199, Arg200, Asn247, Glu414, Gly417, Leu418, Gly508, Tyr542, Lys689 and Tyr690. The specificity of GCPIII towards the P1' glutamate (or glutamate-like moieties) is determined by a combination of ionic and polar interactionsGCPIII substrate-binding cavity structure, overview
-
-
?
additional information
?
-
enzyme/hydroxamate complexes reveal an unprecedented binding mode in which the putative P1' glutarate occupies the spacious entrance funnel rather than the conserved glutamate-binding S1' pocket. This unique binding mode provides a mechanistic explanation for the structure-activity relationship data, most notably the lack of enantiospecificity and the tolerance for bulky/hydrophobic functions as substituents of a canonical glutarate moiety
-
-
?
additional information
?
-
-
enzyme/hydroxamate complexes reveal an unprecedented binding mode in which the putative P1' glutarate occupies the spacious entrance funnel rather than the conserved glutamate-binding S1' pocket. This unique binding mode provides a mechanistic explanation for the structure-activity relationship data, most notably the lack of enantiospecificity and the tolerance for bulky/hydrophobic functions as substituents of a canonical glutarate moiety
-
-
?
additional information
?
-
-
the enzyme interacts with filamin leading to internalization of PMSA into cells in the perinuclear region, overview
-
-
?
additional information
?
-
-
bifunctional enzyme performing folate hydrolase and N-acetylated alpha-linked acidic dipeptidase, NAALADase, activities
-
-
?
additional information
?
-
mouse glutamate carboxypeptidase II possesses lower catalytic efficiency but similar substrate specificity compared with the human protein
-
-
?
additional information
?
-
-
mouse glutamate carboxypeptidase II possesses lower catalytic efficiency but similar substrate specificity compared with the human protein
-
-
?
additional information
?
-
-
enzyme inhibition depresses mossy fiber-CA3 synaptic transmission
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N-acetyl-alpha L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
-
-
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
-
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
-
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
i.e. NAAG, a neurodipeptide, the enzyme acts as membrane-bound receptor being recycled through clathrin coated pits, expression regulation within cells and involvement in prostate cancer and metastasis, overview
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
supply of the primary excitatory neurotransmitter glutamate, the enzyme is involved in neurological disorders, and neuropathic and inflammatory pain
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
the enzyme is involved in glutamate-mediated neurodegenerative disorders, enzyme inhibition is a mechanism for reduction of excitotoxic glutamate
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
the enzyme is involved in suppressing prostate cancer invasiveness
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
the enzyme is responsible for cleavage of NAAG to yield free glutamate
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
the essential enzyme is involved in prostate cancer, stroke, amyotrophic lateral sclerosis, and neuropathic pain
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
-
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
-
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
-
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
i.e. NAAG, a neurodipeptide, the enzyme acts as membrane-bound receptor being recycled through clathrin coated pits, expression regulation within cells in prostate cancer and metastasis, overview
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
the enzyme inactivates the neurotransmitter in the synaptic cleft
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
the enzyme is responsible for glutamate supply, enzyme inhibition decreases the glutamate and increases the N-acetyl-alpha-L-aspartyl-L-glutamate concentration in the brain, which can be a method to treat opioid tolerance and diminish effects of morphine withdrawal, overview
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
the enzyme is responsible for glutamate supply, enzyme inhibition decreases the glutamate and increases the N-acetyl-alpha-L-aspartyl-L-glutamate concentration in the brain, which can be a method to treat opioid tolerance and diminish effects of morphine withdrawal, overview
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
enzyme regulation is mediated by glial glutamate and acetylcholine receptors in the nervous tissue
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
-
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
enzyme inhibition reduces acute neuronal degeneration and astrocyte damage following lateral fluid percussion traumatic brain injury
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
i.e. NAAG, a neurodipeptide, the enzyme acts as membrane-bound receptor being recycled through clathrin coated pits, expression regulation within cells in prostate cancer and metastasis, overview
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
i.e. NAAG, a presynaptically active endogenous neuropeptide which is cleaved by the enzyme in the extracellular space
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
NAAG peptidase inhibitor reduces acute neuronal degeneration and astrocyte damage following lateral fluid percussion TBI in rats
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
supply of the primary excitatory neurotransmitter glutamate
-
-
?
N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
-
the enzyme is involved in glutamate-mediated neurodegenerative disorders, enzyme inhibition is a mechanism for reduction of excitotoxic glutamate
-
-
?
N-acetyl-Asp-Glu + H2O
N-acetyl-Asp + Glu
-
the enzyme converts N-acetylaspartylglutamate from a neuroprotectant to a neurotoxin
-
-
?
N-Acetyl-L-Asp-L-Glu + H2O
?
-
functions as a cell surface peptidase, possibly hydrolzing peptides in prostatic fluid
-
-
?
N-Acetyl-L-Asp-L-Glu + H2O
?
-
may play a role in signaling between non-myelinating Schwann cells and peripheral axons
-
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
L-glutamate + N-acetyl-L-aspartate
-
-
-
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
L-glutamate + N-acetyl-L-aspartate
-
NAALADase, a neuropeptidase that produces the neurotransmitter glutamate and N-acetyl-Laspartate throught hydrolysis of N-acetyl-L-aspartyl-L-glutamate
-
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
L-glutamate + N-acetyl-L-aspartate
-
-
-
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
-
-
-
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
-
-
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
-
-
-
-
?
N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
-
-
-
-
?
additional information
?
-
-
the enzyme interacts with filamin leading to internalization of PMSA into cells in the perinuclear region, overview
-
-
?
additional information
?
-
-
intestinal absorption of polyglutamyl folates involves cleavage of the glutamate side chain by FGCP
-
-
?
additional information
?
-
-
cross-linking of cell surface PSMA with specific antibodies activates the small GTPases RAS and RAC1 and the MAPKs p38 and ERK1/2 in prostate carcinoma LNCaP cells via NF-kappaB activation, overview. Proliferation of LNCaP cells is inducible by interleukin-6, CCL5 or by cross-linking of PSMA
-
-
?
additional information
?
-
-
PSMA is highly homologous to N-acetylated alpha-linked acidic dipeptidase, NAALADase
-
-
?
additional information
?
-
-
PSMA-targeted photodynamic therapy on cytoskeletal networks in prostate cancer cells results in rapid disruption of microtubules (alpha-/beta-tubulin), microfilaments (actin), and intermediate filaments (cytokeratin 8/18) in the cytoplasm of LNCaP cells. The collapse of cytoplasmic microtubules and the later nuclear translocation of alpha-/beta-tubulin are the most dramatic alternation, overview
-
-
?
additional information
?
-
-
the enzyme interacts with filamin leading to internalization of PMSA into cells in the perinuclear region, overview
-
-
?
additional information
?
-
-
enzyme inhibition depresses mossy fiber-CA3 synaptic transmission
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
K+
-
extracellularly applied K+ increases the enzyme activity in vivo in glial cells and the ventral nerve cord
Zn2+
additional information
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
Zn2+
the enzyme contains a binuclear Zn2+ binding site, involved in the reaction mechanism
Zn2+
zinc metallo-enzyme, contains two zinc ions co-ordinated by side chain of His377, Asp387, Glu425, Asp453, His553, which are indispensable for hydrolytic activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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-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-[[[2-[4-(acetylamino)phenyl]ethoxy](hydroxy)phosphoryl]methyl]pentanedioic 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
-
-
(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-5-(1,2-dicarba-closo-dodecarboranylamido) pentyl)ureido)pentanedioic acid
-
(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-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-(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-(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
(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-[1-(2-cyanoethyl)-1H-tetrazol-5-yl]propyl)ureido]pentanedioic acid
-
-
(S)-alpha-ethylglutamate
-
specific group II metabotropic glutamate receptor antagonist, in vivo activity
(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
-
-
2-(3-sulfanylpropyl)pentanedioic acid
-
i.e. GPI-5693, attenuates cocaine-induced conditioned place preference
2-(phosphonomethyl) pentanedioic acid
inhibitor completely blocks N-acetylaspartylglutamate cleavage activity but not Amyloid-beta degradation
2-(phosphonomethyl)pentandioic acid
10fold selectivity compared to glutamate carboxypeptidase III
2-([hydroxy[3-(trifluoromethyl)benzyl]phosphoryl]methyl)pentanedioic acid
-
IC50: 55 nM
2-([hydroxy[hydroxy(phenyl)methyl]phosphoryl]methyl)pentanedioic acid
-
IC50: 55 nM
2-([hydroxy[hydroxy(pyridin-4-yl)methyl]phosphoryl]methyl)pentanedioic acid
-
IC50: 10 nM
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-[(hydroxy[[(4-methoxyphenyl)amino]methyl]phosphoryl)methyl]pentanedioic acid
-
IC50: 3 nM
2-[[(2,4-dicarboxybutyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
-
IC50: 0.5 nM
2-[[(2-carboxy-3-phenylpropyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
-
IC50: 2 nM
2-[[(2-carboxy-4-phenylbutyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
-
IC50: 2 nM
2-[[(2-carboxyethyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
-
IC50: 1 nM
2-[[(2-carboxypropyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
-
IC50: 1.5 nM
2-[[(2-fluorobenzyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
-
IC50: 156 nM
2-[[(3,5-difluorobenzyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
-
IC50: 49 nM
2-[[(3-aminobenzyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
-
IC50: 143 nM
2-[[(3-fluorobenzyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
-
IC50: 70 nM
2-[[(4-fluorobenzyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
-
IC50: 64 nM
2-[[(anilinomethyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
-
IC50: 4 nM
2-[[hydroxy(3-phenylpropyl)phosphoryl]methyl]pentanedioic acid
-
IC50: 230 nM
2-[[hydroxy(4-methoxybenzyl)phosphoryl]methyl]pentanedioic acid
-
IC50: 90 nM
2-[[hydroxy(4-methylbenzyl)phosphoryl]methyl]pentanedioic acid
-
IC50: 68 nM
2-[[hydroxy(pentafluorobenzyl)phosphoryl]methyl]pentanedioic acid
-
IC50: 82 nM. Significantly prevents neurodegeneration in a middle cerebral artery occlusion model of cerebral ischemia. In the chronic constrictive model of neuropathic pain, the inhibitor sifnificantly attenuats the hypersensitivity observed with saline-treated animals
2-[[[(3-fluorophenyl)(hydroxy)methyl](hydroxy)phosphoryl]methyl]pentanedioic acid
-
IC50: 16 nM
2-[[[(benzylamino)methyl](hydroxy)phosphoryl]methyl]pentanedioic acid
-
IC50: 59 nM
2-[[[3,5-bis(trifluoromethyl)benzyl](hydroxy)phosphoryl]methyl]pentanedioic acid
-
IC50: 55 nM
2-[[[3-(benzyloxy)-2-methyl-3-oxopropyl](hydroxy)phosphoryl]methyl]pentanedioic acid
-
IC50: 95 nM
2-{[2-Carboxy-3-(4-methoxy-phenylamino)-propyl]-hydroxy-phosphinoylmethyl}-pentanedioic acid
-
IC50: 3 nM
3-(2-oxotetrahydro-thiopyran-3-yl)propionic acid
-
prodrug of inhibitor 2-(3-mercaptopropyl)pentanedioic acid
3-(3-mercaptopropyl)pentanedioic acid
-
presynaptic action of enzyme inhibition, enzyme inhibition depresses mossy fiber-CA3 synaptic transmission
3-[2-carboxy-3-(hydroxypentafluorophenylmethylphosphinoyl)propyl]benzoic acid
-
IC50: 2400 nM
4-[(2-(R))-2-carboxy-5-(oxidanylamino)-5-oxidanylidene-pentyl]benzoic acid
-
4-[(2-(S))-2-carboxy-5-(oxidanylamino)-5-oxidanylidene-pentyl]benzoic acid
-
4-[[bis[[(isopropoxycarbonyl)oxy]methoxy]phosphoryl]-methyl]-5-[[(isopropoxycarbonyl)oxy]methoxy]-5-oxopentanoic acid
5-oxononane-1,3,7,9-tetracarboxylic acid
-
inhibitor possesses mGluR3 agonist activity
diphenyl 2-[[[2-[4-([[7-(diethylamino)-2-oxo-2H-chromen-3-yl]carbamoyl]amino)phenyl]ethoxy](hydroxy)phosphoryl]methyl]pentanedioate
-
-
DKFZ-PSMA-11
720fold selectivity compared to glutamate carboxypeptidase III
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
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-(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-([(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-[[(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-[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-[[[(1S)-1-carboxy-3-methylbutyl]amino]carbonyl]-L-glutamic acid
i.e. ZJ-43. 160fold selectivity compared to glutamate carboxypeptidase III
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
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
ZJ-43
-
i.e. (S)-2-[3-((S)-1-carboxy-3-methylbutyl)ureido]pentanedioic acid, the inhibitor enhances extracellular NAAG levels and reduces extracellular levels of amino acids neurotransmitter following traumatic brain injury in vivo
(R)-2-(3-mercaptopropyl)-pentanedioic acid
-
equally potent as the S-isomer, 0.000085 mM
(R)-2-(3-mercaptopropyl)-pentanedioic acid
-
antinociceptide effects in the chronic constriction injury model, cell culture model of cerebral ischemia
(R)-2-(hydroxypentafluorophenylmethyl-phosphinoylmethyl)pentanedioic acid
-
40fold less potent than the S-isomer, IC50: 0.0014 mM
(R)-2-(hydroxypentafluorophenylmethyl-phosphinoylmethyl)pentanedioic acid
-
neuroprotective effects in the middle cerebral artery occlusion model, cell culture model of cerebral ischemia
(R)-2-(phosphonomethyl)-pentanedioic acid
-
less potent than the S-isomer, IC50: 0.000030 mM
(S)-2-(3-((S)-1-carboxy-(4-iodobenzamido)pentyl)ureido)pentanedioic acid
DCIBzL
(S)-2-(3-((S)-1-carboxy-(4-iodobenzamido)pentyl)ureido)pentanedioic acid
830fold selectivity compared to glutamate carboxypeptidase III
(S)-2-(3-((S)-1-carboxy-2-(4-hydroxy-3-iodophenyl)ethyl)ureido)pentanedioic acid
DCIT
(S)-2-(3-((S)-1-carboxy-2-(4-hydroxy-3-iodophenyl)ethyl)ureido)pentanedioic acid
-
DCIT
(S)-2-(3-((S)-1-carboxy-5-(3-(4-iodophenyl)ureido)pentyl)ureido)pentanedioic acid
-
i.e. MIP-1095, the compound shows affinity to and uptake into prostate cancer cells, binding analysis, overview
(S)-2-(3-((S)-1-carboxy-5-(3-(4-iodophenyl)ureido)pentyl)ureido)pentanedioic acid
-
-
(S)-2-(3-mercaptopropyl)-pentanedioic acid
-
equally potent as the R-isomer, 0.000067 mM
(S)-2-(3-mercaptopropyl)-pentanedioic acid
-
antinociceptide effects in the chronic constriction injury model, cell culture model of cerebral ischemia
(S)-2-(hydroxypentafluorophenylmethyl-phosphinoylmethyl)pentanedioic acid
-
40fold more potent than the R-isomer, IC50: 0.000034 mM
(S)-2-(hydroxypentafluorophenylmethyl-phosphinoylmethyl)pentanedioic acid
-
neuroprotective effects in the middle cerebral artery occlusion model, cell culture model of cerebral ischemia
(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
-
i.e. inhibitor ZJ17
(S)-2-[3-((S)-1-carboxy-2-(4-hydroxyphenyl)ethyl)ureido]pentanedioic acid
-
i.e. inhibitor ZJ17
(S)-2-[3-((S)-1-carboxy-3-(1H-tetrazol-5-yl)propyl)ureido]pentanedioic acid
-
i.e. inhibitor ZJ38
(S)-2-[3-((S)-1-carboxy-3-(1H-tetrazol-5-yl)propyl)ureido]pentanedioic acid
-
i.e. inhibitor ZJ38
(S)-2-[3-((S)-1-carboxy-3-(methylsulfanyl)propyl)ureido]pentanedioic acid
-
i.e. inhibitor ZJ11
(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-methylbutyl)ureido]pentanedioic acid
-
i.e. inhibitor ZJ43
2-(3-mercaptopropyl)-pentanedioic acid
-
2-MPPA, specific, potent, competitive inhibition, has higher oral bioavailability compared to 2-PMPA, acts neuroprotective in vivo, e.g. in case of ischemic stroke, and provides analgesia
2-(3-mercaptopropyl)-pentanedioic acid
-
2-MPPA, prevents morphine tolerance without affecting the acute morphine antinociception in vivo
2-(3-mercaptopropyl)-pentanedioic acid
-
2-MPPA, specific, potent, competitive inhibition, acts neuroprotective in vivo, e.g. in case of ischemic stroke, and provides analgesia
2-(3-mercaptopropyl)pentanedioic acid
-
IC50: 90 nM. Orally bioavailable in rats
2-(3-mercaptopropyl)pentanedioic acid
-
in rat liver microsomes, 2-(3-mercaptopropyl)pentanedioic acid is gradually produced from 3-(2-oxotetrahydro-thiopyran-3-yl)propionic acid, a thiolactone derived from the compound. 2-(3-Mercaptopropyl)pentanedioic acid is detected in plasma at concentrations well above its IC50 value for GCPII following oral administration of 3-(2-oxotetrahydro-thiopyran-3-yl)propionic acid in rats
2-(phosphonomethyl)-pentanedioic acid
-
2-PMPA, specific, potent, competitive inhibition, acts neuroprotective in vivo, e.g. in case of ischemic stroke, and provides analgesia
2-(phosphonomethyl)-pentanedioic acid
2-PMPA, GCPIII IC50: 94 nM, GCPII IC50: 6.74 nM
2-(phosphonomethyl)-pentanedioic acid
-
2-PMPA, specific GCPII inhibitor, in vivo activity
2-(phosphonomethyl)-pentanedioic acid
-
2-PMPA, specific, potent, competitive inhibition, acts neuroprotective in vivo, e.g. in case of ischemic stroke, and provides analgesia
2-(phosphonomethyl)-pentanedioic acid
-
i.e. 2-PMPA, enzyme inhibition protects the rats in vivo against ischemic injury to the brain and spinal cord, and hypoxic and metabolic injury to neuronal cells in culture
2-(phosphonomethyl)pentanedioic acid
-
potent inhibitor, robust neuroprotective efficacy in many neurological disease models
2-(phosphonomethyl)pentanedioic acid
completely blocks the NAAG hydrolysis without any effect on amyloid-beta degradation
2-(phosphonomethyl)pentanedioic acid
potent inhibitor, robust neuroprotective efficacy in many neurological disease models
2-(phosphonomethyl)pentanedioic acid
-
i.e. 2-PMPA, inhibits cocaine-induced behavioural sensitization
2-(phosphonomethyl)pentanedioic acid
-
i.e. 2-PMPA, a N-acetylated-alpha-linkedacidic dipeptidase inhibitor, attenuates cocaine self-administration and cocaine-induced reinstatement of drug seeking of rats
2-[[hydroxy(2-phenylethyl)phosphoryl]methyl]pentanedioic acid
-
IC50: 150 nM
2-[[hydroxy(2-phenylethyl)phosphoryl]methyl]pentanedioic acid
-
IC50: 149 nM
4,4'-phosphinicobis(butane-1,3-dicarboxylic acid)
-
i.e. PBDA, effects of stereoisomers, overview
4-[[bis[[(isopropoxycarbonyl)oxy]methoxy]phosphoryl]-methyl]-5-[[(isopropoxycarbonyl)oxy]methoxy]-5-oxopentanoic acid
-
the orally bioavailable prodrug affords excellent release of 2-phosphonomethylpentanedioic acid following oral administration in both mice and dog
4-[[bis[[(isopropoxycarbonyl)oxy]methoxy]phosphoryl]-methyl]-5-[[(isopropoxycarbonyl)oxy]methoxy]-5-oxopentanoic acid
the orally bioavailable prodrug affords excellent release of 2-phosphonomethylpentanedioic acid following oral administration in both mice and dog
GPI5232
-
i.e. 2-([((hydroxypentyfluorophenyl)methyl)phosphinoyl]methyl)pentanedioic acid
GPI5232
-
i.e. 2-([((hydroxypentyfluorophenyl)methyl)phosphinoyl]methyl)pentanedioic acid
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-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, agonist and antagonist activity on recombinantly expressed metabotropic glutamate receptor, 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-(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, agonist and antagonist activity on recombinantly expressed metabotropic glutamate receptor, 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
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, agonist and antagonist activity on recombinantly expressed metabotropic glutamate receptor, overview
N-[[(1S)-1-carboxy-5-(4-iodobenzamido)pentyl]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)-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-([(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-[acetyl[(4-bromophenyl)methyl]amino]-1-carboxypentyl]carbamoyl]-L-glutamic acid
-
N-[[(1S)-5-[acetyl[(4-bromophenyl)methyl]amino]-1-carboxypentyl]carbamoyl]-L-glutamic acid
-
additional information
-
the androgen receptor negatively regulates the enzyme expression
-
additional information
-
design of urea-based NAAG peptidase-specific inhibitors, IC50 values of the stereoisomers, inhibition strategies, overview, inhibitors are used in therapy of neurological disorders, overview, construction of a human traumatic brain injury, TBI, to test inhibitor effects, overview
-
additional information
-
GCPIII enzyme-inhibitor interactions and the architecture of the S1' pocket, overview
-
additional information
-
design and synthesis of a series of glutamate-urea-X heterodimeric inhibitors of PSMA, where X is epsilon-N-(o-I, m-I, p-I, p-Br, o-Cl, m-Cl, p-Cl, p-F, H)-benzyl-Lys and epsilon-(p-I, p-Br, p-Cl, p-F, H)-phenylureido-Lys, overview. PSMA binding of the benzyllysine series is significantly affected by the nature of the halogen substituent. The halogen atom has little affect on the binding affinity in the para-substituted phenylureido-Lys series
-
additional information
-
inhibitor in vivo distribution studies in mice bearing either PSMA-positive LNCaP or PSMA-negative PC-3 tumors, overview
-
additional information
-
phosphoramidate peptidomimetic PSMA inhibitors are capable of both cell-surface labeling of prostate cancer cells and intracellular delivery. Use of a PSMA inhibitor-conjugate of pyropheophorbide-a, i.e. Ppa-conjugate 2, for targeted photodynamic therapy to achieve apoptosis in PSMA and LNCaP cells, overview
-
additional information
pharmacophore analysis followed by QSAR studies proposes a N-acetyl aspartyl glutamate-analogue as the most potent inhibitor of the enzyme, effective across all the genetic variants of glutamate carboxypeptidase II. This molecule satisfies Lipinski rule of five and rule of three for drug-likeliness. Being a N-acetyl aspartyl glutamate-analogue, this molecule might confer neuroprotection by inhibiting glutamatergic neurotransmission mediated by N-acetylated alpha-linked acidic dipeptidase (NAALADase), a splice variant of glutamate carboxypeptidase II
-
additional information
-
the androgen receptor negatively regulates the enzyme expression
-
additional information
-
N-[N-((S)-1,3-dicarboxypropyl)carbamoyl]-S-3-iodo-L-tyrosine, i.e. DCIT, is a potent antagonist of the enzyme activity
-
additional information
-
glutamate receptor antagonists reduce the enzyme activity in vivo, overview
-
additional information
-
not inhibitory are pepstatin, iodoacetamide, amastatin
-
additional information
-
GCPII inhibitors are attractive candidates for clinical treatment trials in amylotrophic lateral sclerosis
-
additional information
-
design of urea-based NAAG peptidase-specific inhibitors, inhibition strategies, overview, construction of a stroke rat model and traumatic brain injury, TBI, to test inhibitor effects, overview
-
additional information
-
N-[N-((S)-1,3-dicarboxypropyl)carbamoyl]-S-3-iodo-L-tyrosine, i.e. DCIT, is a potent antagonist of the enzyme activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.00129
(2S,2'S,4R,4'R)-N,N'-carbonyl-4,4'-dimethyldiglutamic acid
-
pH 7.4, 37°C, recombinant enzyme
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
0.000000003
(S)-2-(3-((S)-1-carboxy-(4-iodobenzamido)pentyl)ureido)pentanedioic acid
pH and temperature not specified in the publication
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
-
-
0.000000049
(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
0.000003
(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
0.000008
(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
0.00000028
2-(phosphonomethyl)pentandioic acid
pH and temperature not specified in the publication
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
0.0000149
N-[[(1S)-1-carboxy-3-(1H-tetrazol-5-yl)propyl]carbamoyl]-L-glutamic acid
-
pH 7.4, 37°C
0.000000017 - 0.000000028
N-[[(1S)-1-carboxy-5-(4-iodobenzamido)pentyl]carbamoyl]-L-glutamic acid
0.000000018 - 0.0000001
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
0.000000021 - 0.000000049
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
0.00000005 - 0.00000068
N-[[(1S)-5-[acetyl[(4-bromophenyl)methyl]amino]-1-carboxypentyl]carbamoyl]-L-glutamic acid
0.00000058
N-[[[(1S)-1-carboxy-3-methylbutyl]amino]carbonyl]-L-glutamic acid
pH and temperature not specified in the publication
0.00052
(2S)-2-amino-3-(3,5-dioxo-1,2,4-oxadiazolidin-2-yl)propanoic acid
37°C, pH 7.4
0.00058
(2S)-2-amino-3-(3,5-dioxo-1,2,4-oxadiazolidin-2-yl)propanoic acid
37°C, pH 7.4
0.000095
(2S,2'S,4R)-4-benzyl-N,N'-carbonyldiglutamic acid
-
pH 7.4, 37°C, recombinant enzyme
0.000392
(2S,2'S,4R,4'R)-4,4'-dibenzyl-N,N'-carbonyldiglutamic acid
-
pH 7.4, 37°C
0.000392
(2S,2'S,4R,4'R)-4,4'-dibenzyl-N,N'-carbonyldiglutamic acid
-
pH 7.4, 37°C, recombinant enzyme
0.000014
(2S,2'S,4S)-N,N'-carbonyl-4-methyldiglutamic acid
-
pH 7.4, 37°C, recombinant enzyme
0.0000129
(2S,3'S)-[[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl]-pentanedioic acid
-
GCPII
0.0000346
(2S,3'S)-[[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl]-pentanedioic acid
-
GCPIII
0.0000021
(S)-2-[3-((S)-alpha-carboxybenzyl)ureido]pentanedioic acid
-
pH 7.4, 37°C
0.0000021
(S)-2-[3-((S)-alpha-carboxybenzyl)ureido]pentanedioic acid
-
pH 7.4, 37°C, recombinant enzyme
0.00443
(S,S)-4,4'-bis[1-(2-cyanoethyl)-1H-tetrazol-5-yl]-2,2'-ureylenedibutyric acid
-
pH 7.4, 37°C, recombinant enzyme
0.004434
(S,S)-4,4'-bis[1-(2-cyanoethyl)-1H-tetrazol-5-yl]-2,2'-ureylenedibutyric acid
-
pH 7.4, 37°C
0.000939
(S,S)-N,N'-carbonyl-2,2'-dimethyldiglutamic acid
-
pH 7.4, 37°C, recombinant enzyme
0.0000014
2-(phosphonomethyl)-pentanedioic acid
-
pH 7.4, 37°C, recombinant enzyme
0.0000003
2-(phosphonomethyl)pentanedioic acid
-
pH and temperature not specified in the publication
0.0000003
2-(phosphonomethyl)pentanedioic acid
pH and temperature not specified in the publication
0.016
N-[4-carboxy-3-(carboxymethyl)-3-hydroxybutanoyl]-L-glutamic acid
37°C, pH 7.4
0.024
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
0.0000059
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
0.000000028
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
0.0000001
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
0.000000049
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
0.00000066
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
0.00000068
N-[[(1S)-5-[acetyl[(4-bromophenyl)methyl]amino]-1-carboxypentyl]carbamoyl]-L-glutamic acid
37°C, pH 7.4
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.000017
(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
-
0.000245
(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
-
-
0.000034
(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
0.00009
2-(3-mercaptopropyl)pentanedioic acid
Rattus norvegicus
-
IC50: 90 nM. Orally bioavailable in rats
0.000175
2-(phosphonomethyl)-4-(5H-tetrazol-5-yl)butanoic acid
Rattus norvegicus
-
IC50: 175 nM
0.000055
2-([hydroxy[3-(trifluoromethyl)benzyl]phosphoryl]methyl)pentanedioic acid
Rattus norvegicus
-
IC50: 55 nM
0.000055
2-([hydroxy[hydroxy(phenyl)methyl]phosphoryl]methyl)pentanedioic acid
Rattus norvegicus
-
IC50: 55 nM
0.00001
2-([hydroxy[hydroxy(pyridin-4-yl)methyl]phosphoryl]methyl)pentanedioic acid
Rattus norvegicus
-
IC50: 10 nM
0.000003
2-[(hydroxy[[(4-methoxyphenyl)amino]methyl]phosphoryl)methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 3 nM
0.0000005
2-[[(2,4-dicarboxybutyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 0.5 nM
0.000002
2-[[(2-carboxy-3-phenylpropyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 2 nM
0.000002
2-[[(2-carboxy-4-phenylbutyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 2 nM
0.000001
2-[[(2-carboxyethyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 1 nM
0.0000015
2-[[(2-carboxypropyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 1.5 nM
0.000156
2-[[(2-fluorobenzyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 156 nM
0.000049
2-[[(3,5-difluorobenzyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 49 nM
0.000143
2-[[(3-aminobenzyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 143 nM
0.00007
2-[[(3-fluorobenzyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 70 nM
0.000064
2-[[(4-fluorobenzyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 64 nM
0.000004
2-[[(anilinomethyl)(hydroxy)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 4 nM
0.000059
2-[[hydroxy(3-nitrobenzyl)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50 59 nM
0.00023
2-[[hydroxy(3-phenylpropyl)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 230 nM
0.00009
2-[[hydroxy(4-methoxybenzyl)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 90 nM
0.000068
2-[[hydroxy(4-methylbenzyl)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 68 nM
0.000082
2-[[hydroxy(pentafluorobenzyl)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 82 nM. Significantly prevents neurodegeneration in a middle cerebral artery occlusion model of cerebral ischemia. In the chronic constrictive model of neuropathic pain, the inhibitor sifnificantly attenuats the hypersensitivity observed with saline-
0.00293
2-[[hydroxy(phenyl)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 2930 nM
0.000016
2-[[[(3-fluorophenyl)(hydroxy)methyl](hydroxy)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 16 nM
0.000059
2-[[[(benzylamino)methyl](hydroxy)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 59 nM
0.000055
2-[[[3,5-bis(trifluoromethyl)benzyl](hydroxy)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 55 nM
0.000095
2-[[[3-(benzyloxy)-2-methyl-3-oxopropyl](hydroxy)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 95 nM
0.000003
2-{[2-Carboxy-3-(4-methoxy-phenylamino)-propyl]-hydroxy-phosphinoylmethyl}-pentanedioic acid
Rattus norvegicus
-
IC50: 3 nM
0.002
3-(2-oxotetrahydro-thiopyran-3-yl)propionic acid
Rattus norvegicus
-
pH not specified in the publication, temperature not specified in the publication
0.0024
3-[2-carboxy-3-(hydroxypentafluorophenylmethylphosphinoyl)propyl]benzoic acid
Homo sapiens
-
IC50: 2400 nM
0.000508
4-(3-hydroxyphenyl)-2-(phosphonomethyl)butanoic acid
Rattus norvegicus
-
IC50: 508 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
-
-
0.000016
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
0.000007
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
-
-
0.0018
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
0.000014
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
-
-
0.00000674
2-(phosphonomethyl)-pentanedioic acid
Mus musculus
2-PMPA, GCPIII IC50: 94 nM, GCPII IC50: 6.74 nM
0.000094
2-(phosphonomethyl)-pentanedioic acid
Mus musculus
2-PMPA, GCPIII IC50: 94 nM, GCPII IC50: 6.74 nM
0.000053
2-[[benzyl(hydroxy)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 53 nM
0.00007
2-[[benzyl(hydroxy)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 70 nM
0.000149
2-[[hydroxy(2-phenylethyl)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 149 nM
0.00015
2-[[hydroxy(2-phenylethyl)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 150 nM
0.00036
2-[[hydroxy(propyl)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 360 nM
0.00056
2-[[hydroxy(propyl)phosphoryl]methyl]pentanedioic acid
Rattus norvegicus
-
IC50: 560 nM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
activity in prostate tissue homogenate in comparison to other species, overview
additional information
-
activity in prostate tissue homogenate in comparison to other species, overview
additional information
-
activity in prostate tissue homogenate in comparison to other species, overview
additional information
-
activity in prostate tissue homogenate in comparison to other species, overview
additional information
-
activity in prostate tissue homogenate in comparison to other species, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
-
731253, 731257, 731449, 731778, 731799, 732852, 752647, 752648, 752675, 752980, 753547, 753551, 753584, 754372, 754380, 754505, 755286, 755336
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
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
brenda
-
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
brenda
-
higher level in patients with prostrate cancer, lower levels in healthy male donors
brenda
additional information
the level of glutamate carboxypeptidase II protein (GCPII) is regulated by valproic acid, a histone deacetylase (HDAC) inhibitor, through acetylation of lysine residue in the GCPII protein in human astrocytes, U-87MG
brenda
-
decreased gene expression and activity in the frontal and temporal lobe, the dorsolateral prefrontal cortex, and the hippocampus in schizophrenia, overview, no intracellular activity in pyramidal cells and their dendrites
brenda
-
especially midbrain and cerebellum, quantitative detection of GCPII content in the brain by labeling with [125I]-N-[N-((S)-1,3-dicarboxypropyl)carbamoyl]-S-3-iodo-L-tyrosine is a potent antagonist of the enzyme activity
brenda
-
-
brenda
-
amygdala, caudate-putamen, central gray, dorsal raphe, globus pallidus, hippocampus, hypothalamus, locus coerulus, medial and lateral geniculate, olfactory bulb, periaqueductal gray, solitary nucleus, spinal trigeminal nucleus, substantia nigra, superior colliculus, thalamus, corpus callosum, fornix, habenular commissure, solitary tract, stria medularis, stria therminalis
brenda
-
especially midbrain and cerebellum, quantitative detection of GCPII content in the brain by labeling with [125I]-N-[N-((S)-1,3-dicarboxypropyl)carbamoyl]-S-3-iodo-L-tyrosine is a potent antagonist of the enzyme activity
brenda
-
kidney cortex, specifically in the brush border of proximal convoluted tubules
brenda
-
-
brenda
-
originating from a prostate cancer lymph node metastasis
brenda
withdrawal of 3,4-methylenedioxypyrovalerone reduces expression of glutamate carboxypeptidase II in the prefrontal cortex
brenda
-
-
brenda
-
high PSMA expression level, overexpression in advanced stage prostate adenocarcinomas. PSMA expression analysis and distribution pattern of PSMA in primary and metastatic tumors, immunohistochemic detection, overview
brenda
-
PSMA is a transmembrane protein commonly found on the surface of late-stage and metastatic prostate cancer
brenda
-
prostrate carcinoma cell line LNCaP
brenda
-
prostate form of the enzyme is termed prostate-specific membrane antigen
brenda
highly expressed, might be associated with prostate cancer progression
brenda
-
prostatic adenocarcinoma and intraepithelial neoplasia
brenda
-
lymph node metastasis, PSMA is highly expressed in 100% of the lymph node metastases originating from prostate cancer
brenda
considerably increased in prostate carcinoma
brenda
-
expressed during late embryonal and early postnatal development. During the first prenatal week the enzyme is downregulated in myelinating Schwann cells while the total enzyme concentrations in the nerves are transiently increased
brenda
the level of glutamate carboxypeptidase II protein (GCPII) is regulated by valproic acid, a histone deacetylase (HDAC) inhibitor, through acetylation of lysine residue in the GCPII protein in human astrocytes, U-87MG
brenda
additional information
-
analysis of enzyme expression in prostate tissue during carcinoma development
brenda
additional information
-
no activity in the PSMA-negative prostate cancer cell line DU 145
brenda
additional information
-
quantitative PSMA expression analysis in cancer cell lines and tissues, overview
brenda
additional information
-
quantitative PSMA expression analysis in cancer cells, overview
brenda
additional information
tissue distribution of GCPIII activity and expression, overview
brenda
additional information
-
tissue distribution of GCPIII activity and expression, overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
Vinca alkaloids destabilize the microtubules leading to basolateral expression of the enzyme and its integration into the basolateral membrane
-
brenda
-
PSMA is a transmembrane protein commonly found on the surface of late-stage and metastatic prostate cancer
brenda
-
present in neurophil cytoplasm, absent from neuronal cytoplasm
brenda
-
-
137212, 137218, 137226, 667114, 668484, 668866, 670740, 697394, 701206, 707988, 710007, 710456, 710458, 710460, 710658
brenda
-
the enzyme is associated with the cell surface membrane. The recombinant enzyme and the mutant enzyme omitting the transmembrane domain is associated with the cell surface membrane, the recombinantly expressed extracellular domain has a cytosolic localization
brenda
-
PSMA is a transmembrane protein commonly found on the surface of late-stage and metastatic prostate cancer
brenda
-
-
brenda
-
direct targeting of the enzyme to the apical plasma membrane, correct sorting into appropriate post-Golgi vesicles depends on the N-glycosylation of the enzyme, integrity of the microtubule skeleton is required for enzyme localization in the apical plasma membrane
brenda
-
the enzyme is a type II membrane glycoprotein with an intracellular segment, a transmembrane domain, and an extensive extracellular domain
brenda
-
the enzyme is a type II membrane glycoprotein with an intracellular segment, a transmembrane domain, and an extensive extracellular domain
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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
malfunction
-
involvement of the endogenous NAAG-NAALADase signaling pathway in cocaine addiction. Inhibition of NAALADase by 2-PMPA attenuates cocaine-induced relapse in rats via a NAAG-mGluR2/3-mediated mechanism, overview
malfunction
the enzyme is involved in neurological disorders and overexpressed in a number of solid cancers
physiological function
-
PSMA acts as a glutamate-preferring carboxypeptidase in human prostate tissue, and plays a role in folic acid utilization and metabolism
physiological function
Amp1 mutants display hypersensitivity to abscisic acid, while overexpression of Amp1 causes insensitivity to abscisic acid. Endogenous abscisic acid concentration is increased in Amp1 mutant and decreased in Amp1-overexpressing plants under stress conditions. Application of abscisic acid reduces the Amp1 protein level in plants. Amp1 mutants accumulate excess superoxide and displaye hypersensitivity to oxidative stress. The hypersensitivity of Amp1 mutants to abscisic acid and oxidative stress is partially rescued by reactive oxygen species scavenging agents. Amp1 mutants are tolerant to freezing and drought stress. The abscisic acid hypersensitivity and freezing tolerance of Amp1 mutants are dependent on abscisic acid signaling. Amp1 mutants show elevated soluble sugar content and show hypersensitivity to high concentrations of sugar. The contents of amino acids are changed in Amp1 mutants compared to the wild-type
physiological function
glutamate carboxypeptidase II has a physiological function in degrading amyloid-beta. Amyloid-beta degradation occurs through S1 pocket but not through S1' pocket responsible for N-acetylaspartylglutamate hydrolysis. Treatment with a S1 pocket-specific chemical inhibitor prevents GCPII from amyloid-beta degradation without any impairment in N-acetylaspartylglutamate hydrolysis. Likewise, specific GCPII inhibitor 2-(phosphonomethyl) pentanedioic acid developed targeting S1' pocket completely blocks the N-acetylaspartylglutamate hydrolysis without any effect on amyloid-beta degradation. Pre-incubation with N-acetylaspartylglutamate and amyloid-beta does not affect amyloid-beta degradation and N-acetylaspartylglutamate hydrolysis, respectively
physiological function
glutamate carboxypeptidase II is not an amyloid peptide-degrading enzyme
physiological function
the enzyme participates in glutamate excitotoxicity in the brain
Show AA Sequence and Transmembrane Helices (189 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
84000
-
calculation from sequence of cDNA, short intracellular domain, single transmembrane element, large glubular extracellular domain
84490
-
sequence of cDNA, nonglycosylated enzyme form, the extracellular domain contains nine potential N- glycosylation sites
additional information
-
domain structure, sequence alignment with transferrin receptor, the catalytic domain can be assigned to the peptidase family M28
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
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
additional information
additional information
-
the enzyme is monomeric or dimeric a type II membrane glycoprotein with an intracellular segment of amino acid residues 1-18, a transmembrane domain of residues 19-43, and an extensive extracellular domain comprising residues 44-750
additional information
-
the enzyme posseses an extracellular domain, a transmembrane segment, and a cytoplasmic tail
additional information
-
overall fold and quaternary arrangement of the GCPIII molecule, overview
additional information
-
the PSMA protein has intracellular, transmembrane and extracellular domains
additional information
-
the enzyme is a is monomeric or dimeric type II membrane glycoprotein with an intracellular segment, a transmembrane domain, and an extensive extracellular domain
additional information
-
the enzyme is a type II membrane glycoprotein with an intracellular segment, a transmembrane domain, and an extensive extracellular domain
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
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
-
identification of the N-glycosylation sites, e.g. N121, N153, N195, N638, and N140, the enzyme is heavily glycosylated
glycoprotein
-
N-glycosylation, correct sorting into appropriate post-Golgi vesicles for targeting into the apical plasma membrane depends on the N-glycosylation of the enzyme, inhibition of N-glycosylation abolishes the polarized enzyme expression, overview
glycoprotein
-
type II transmembrane glycoprotein, N- and O-glycosylation, mannose-rich glycosylation renders the enzyme trypsin-insensitive, which is typical for Golgi-located enzyme, overview
glycoprotein
-
the extracellular domain contains nine potential glycosylation sites
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
E424A
H475Y
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
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
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
T640A
-
site-directed mutagenesis of an N-glycosylation site, nearly inactive enzyme
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
additional information
E424A
catalytically inactive, series of X-ray structures of complexes a panel of naturally occurring polyglutamylated folates
H475Y
-
C1561T single nucleotide polymorphism located in the putative catalytic region of the enzyme
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
N336A
-
site-directed mutagenesis of an N-glycosylation site leads to 45% reduced activity compared to the wild-type enzyme
N336A
-
site-directed mutagenesis, glycosylation site E mutant, inactive mutant, no endocytic internalization
N476A
-
site-directed mutagenesis of an N-glycosylation site leads to 70% reduced activity compared to the wild-type enzyme
N476A
-
site-directed mutagenesis, glycosylation site E mutant, inactive mutant, no iendocytic nternalization
N638A
-
site-directed mutagenesis of an N-glycosylation site, nearly inactive enzyme
additional information
-
antitumor immune respone in female C57BL/6 (H-2kb) mice to DNA vaccine and efficiency of truncated human prostate-specific membrane antigen can be can be enhanced by a genetically enhanced adjuvant 4-1BB ligand [4-1BBL] from mouse, overview
additional information
downregulation of prostate-specific membrane antigen expression by lentivirus-mediated RNA interference significantly suppresses the growth rates of LNCaP and DU-145 cells. The specific down-regulation arrests cells in G0/G1 phase of cell cycle
additional information
-
highly efficient capture and enumeration of low abundance prostate cancer cells using prostate-specific membrane antigen aptamers immobilized to a polymeric microfluidic device, method development and evaluation, overview. PSMA can be used as a marker to select these cells from highly heterogeneous clinical samples, selective isolation of rare circulating prostate tumor cells resident in a peripheral blood matrix, overview
additional information
-
in vivo detection of PSMA-positive tumors in mice by labeled monoclonal antibodies, method development and evaaluation, overview
additional information
-
synthesis of a series of PSMA-targeted 99mTc-chelate complexes for imaging PSMA-expressing human prostate cancer cells, in silico docking studies using the crystal structure of PSMA, overview. Synthesis of core ligand 2-[3-(3-benzyloxycarbonyl-1-tert-butoxycarbonyl-propyl)-ureido]pentanedioic acid di-tert-butyl ester and deprotected core ligand 2-[3-(1,3-bis-tert-butoxycarbonyl-propyl)-ureido]pentanedioic acid 1-tert-butyl ester
additional information
synthesis of a series of PSMA-targeted 99mTc-chelate complexes 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 PSMA-targeted chemotherapy. Molecular dynamics, overview
additional information
-
synthesis of a series of PSMA-targeted 99mTc-chelate complexes 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 PSMA-targeted chemotherapy. Molecular dynamics, overview
additional information
-
the PSMA splice variant of the protein remains intracellular without extracellular domain
additional information
-
usage of the ectodomain of PSMA as target for a retargeted measles virus, that harbors a single-chain antibody specific for the extracellular domain of PSMA (J591) inserted as a C-terminal extension on its viral attachment protein. Live attenuated vaccine strain of measles virus has promising antitumor activity. Fully retargetedMVthat infects cells exclusively through the PSMA receptor, which is overexpressed on prostate cancer cells and tumor neovasculature, method, overview. Stable transfection of LNCaP cells. The construct leads to tumor regression
additional information
GCPII knockout mutant mice do not show an altered phenotype
additional information
-
GCPII knockout mutant mice do not show an altered phenotype
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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.
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
efficient one-step purification method yields purified recombinant enzyme
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
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
efficient one-step purification method yields purified recombinant enzyme
efficient one-step purification method yields purified recombinant enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a 20.7 kb gene fragment encoding exons 1-3 is subcloned and analyzed by restriction mapping
-
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
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 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 of the full-length enzyme and the mutant enzymes DEALTA20-42 and DELTA1-42 in HEK293 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
-
gene Naalad2, DNA and amino acid sequence determination and analysis, expression of GCPIII in CHO cells
gene PMSA, DNA sequence variants analysis, expression regulation by PMSA enhancer, PSME, involving Ca2+, overview
-
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
-
the extracellular part, amino acids 44-750, of human GCPII is cloned and heterologously overexpressed in Drosophila Schneiders S2 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
Lentivirus-mediated RNAi inhibits PSMA mRNA and protein expression in LNCaP and DU-145 cells, PSMA RNAi induces the changes of cell cycle, overview
withdrawal of 3,4-methylenedioxypyrovalerone reduces expression of glutamate carboxypeptidase II in the prefrontal cortex
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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
diagnostics
-
the enzyme, prostate-specific membrane antigen, is a good marker for prostate cancer
diagnostics
-
PSMA is a well-known imaging biomarker for staging and monitoring therapy, assessment of an 18F-labeled phosphoramidate peptidomimetic as a PSMA-targeted imaging agent for prostate cancer
diagnostics
-
PSMA overexpression in prostate cancer patients is related to a worse prognosis
diagnostics
the enzyme is an important diagnostic marker of prostate cancer progression
medicine
-
detection of cancerous cells in prostrate or blood, target for diagnostic and therapeutic strategies in prostrate cancer, immunotherapy, antibody therapy
medicine
-
design of inhibitors may lead to effective neuroprotective agents, possibility to employ GCPII inhibitors in stroke therapy
medicine
-
GCPII inhibitors are attractive candidates for clinical treatment trials in amylotrophic lateral sclerosis
medicine
-
inhibitors of NAADLADase protect against chronic glutamate-mediated motor neuron degeneration and may prove therapeutic towards amyotrophic lateral sclerosis
medicine
-
NAALADase inhibition may provide a new aproach for the treatment of both neurodegenerative disorders and peripheral neuropathies
medicine
-
the enzyme is an important marker in the diagnosis of prostate cancer
medicine
-
for establishing new strategies to treat peripheral neuropathies
medicine
glutamate carboxypeptidase II is a therapeutic target for neurodegeneration and prostate cancer
medicine
-
glutamate carboxypeptidase II may represent a viable therapeutic target for intervention on psychiatric disease
medicine
-
maternal total homocysteine concentration is affected by C1561T polymorphism, maternal GCPII C1561T variant is associated with neonatal methylmalonic acid concentration
medicine
urea-based, low molecular weight ligands of glutamate carboxypeptidase II have demonstrated efficacy in various models of neurological disorders and can serve as imaging agents for prostate cancer
medicine
-
enzyme is recognized as a major antigen during histoplasmosis. The titer against N-acetylated alpha-linked acidic dipeptidase is significantly increased in the patient sera
medicine
glutamate carboxypeptidase II is present in human blood, and its concentration within a healthy population varies between 1.3 and 17.2 ng/ml in volunteers not diagnosed with prostate cancer
medicine
glutamate carboxypeptidase II is effective in preclinical models of neurological disorders associated with excessive activation of glutamatergic systems. The study validates the use of hydroxamate-based inhibitors in the treatment of a chronic neurological disorder such as neuropathic pain
medicine
-
inhibitors of glutamate carboxypeptidase II with distinct chemical scaffolds are efficacious in several neurological models wherein excess glutamatergic transmission is presumed pathogenic. These include animal models of neuropathic pain, peripheral neuropathy, stroke, amyotrophic lateral sclerosis, multiple sclerosis, schizophrenia, epilepsy, traumatic brain injury, addiction, and cognition
medicine
inhibitors of glutamate carboxypeptidase II with distinct chemical scaffolds are efficacious in several neurological models wherein excess glutamatergic transmission is presumed pathogenic. These include animal models of neuropathic pain, peripheral neuropathy, stroke, amyotrophic lateral sclerosis, multiple sclerosis, schizophrenia, epilepsy, traumatic brain injury, addiction, and cognition
medicine
the enzyme is a putative target for the treatment of both prostate cancer and neuronal disorders associated with glutamate excitotoxicity
medicine
the enzyme is a reliable in vivo marker of re-endothelialisation after percutaneous vascular intervention and that glutamate carboxypeptidase II-positron emission tomography is the first non-invasive in vivo molecular imaging technique that can demonstrate and quantify re-endothelialisation. As a further perspective, well-powered studies in patients undergoing percutaneous vascular intervention need to confirm the potential of GCPII-PET for imaging the crucial process of arterial re-endothelialisation after injuring the vessel wall
medicine
the enzyme is an important diagnostic marker of prostate cancer progression and a putative target for the treatment of both prostate cancer and neuronal disorders associated with glutamate excitotoxicity. For the development of novel therapeutics, mouse models are used. Differences in enzymatic activity and inhibition profile are small. Therefore, mouse glutamate carboxypeptidase II can approximate human glutamate carboxypeptidase II in drug development and testing. On the other hand, significant differences in glutamate carboxypeptidase II tissue expression must be taken into account when developing novel glutamate carboxypeptidase II-based anticancer and therapeutic methods, including targeted anticancer drug delivery systems, and when using mice as a model organism
medicine
-
enzyme is recognized as a major antigen during histoplasmosis. The titer against N-acetylated alpha-linked acidic dipeptidase is significantly increased in the patient sera
-
pharmacology
-
enzyme inhibitors are used in therapy of neruological disorders, overview
pharmacology
the enzyme is a drug target in neuronal damage and prostate cancer
pharmacology
-
the enzyme is a target for specific inhibitor design in therapy of neurodegenerative disorders, overview
pharmacology
-
the enzyme NAALADase is a target for drug treatment in neuropathic pain
pharmacology
-
effects of PSMA-targeted photodynamic therapy on cytoskeletal networks in prostate cancer cells
pharmacology
-
PSMA is a target for imaging and therapeutic applications for prostate cancer
pharmacology
-
usage of the ectodomain of PSMA as target for a retargeted measles virus, that harbors a single-chain antibody specific for the extracellular domain of PSMA (J591) inserted as a C-terminal extension on its viral attachment protein. Live attenuated vaccine strain of measles virus has promising antitumor activity. Fully retargeted MV that infects cells exclusively through the PSMA receptor, which is overexpressed on prostate cancer cells and tumor neovasculature, method, overview. The construct leads to tumor regression
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EXTERNAL LINKS (specific for EC-Number 3.4.17.21)
Transporter Classification Database (TCDB): 9.B.229.1.5
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Release 2023.1 (January 2023)
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