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amyloid-beta + H2O
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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
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folyl-(gamma-L-glutamic acid)2 + H2O
folyl-gamma-L-glutamic acid + L-glutamate
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folyl-(gamma-L-glutamic acid)3 + H2O
folyl-(gamma-L-glutamic acid)2 + L-glutamate
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folyl-(gamma-L-glutamic acid)4 + H2O
folyl-(gamma-L-glutamic acid)3 + L-glutamate
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folyl-gamma-L-glutamic acid + H2O
folate + L-glutamate
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folyl-poly-gamma-glutamate + H2O
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cleavage of the C-terminal glutamate
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gamma-L-Glu-L-Glu + H2O
L-Glu + L-Glu
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L-Asp-L-Glu + H2O
L-Asp + L-Glu
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L-Glu-L-Glu + H2O
L-Glu + L-Glu
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methotrexate triglutamate + H2O
L-Glu + methotrexate
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N-acetyl-alpha L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
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N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
N-acetyl-Asp-Glu + H2O
N-acetyl-Asp + Glu
N-Acetyl-L-Asp-L-Glu + H2O
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N-Acetyl-L-Asp-L-Glu + H2O
N-Acetyl-L-Asp + L-Glu
N-acetyl-L-aspartyl-L-glutamate
N-acetyl-L-aspartate + L-glutamate
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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-[4-(phenylazo)-benzoyl]-L-glutamyl-gamma-L-glutamic acid + H2O
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poly-gamma-glutamate folate + H2O
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poly-gamma-Glutamylfolate + H2O
L-Glu + gamma-glutamylfolate
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removes sequentially gamma-linked glutamates
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pteroyl-di-L-glutamate + H2O
L-Glu + pteroylglutamate
pteroylpentaglutamate + H2O
L-Glu + pteroylglutamate
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additional information
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N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
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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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N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
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N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
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enantiospecific reaction
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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, 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
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N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
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supply of the primary excitatory neurotransmitter glutamate, the enzyme is involved in neurological disorders, and neuropathic and inflammatory pain
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N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
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the enzyme is involved in glutamate-mediated neurodegenerative disorders, enzyme inhibition is a mechanism for reduction of excitotoxic glutamate
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N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
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the enzyme is involved in suppressing prostate cancer invasiveness
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N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
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the enzyme is responsible for cleavage of NAAG to yield free glutamate
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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
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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
i.e. NAAG
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N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
i.e. NAAG, C-terminal glutamate recognition
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N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
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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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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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N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
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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
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N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
the enzyme inactivates the neurotransmitter in the synaptic cleft
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N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
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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
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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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
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N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
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enantiospecific reaction
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N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
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enzyme inhibition reduces acute neuronal degeneration and astrocyte damage following lateral fluid percussion traumatic brain injury
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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, 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
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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, a presynaptically active endogenous neuropeptide which is cleaved by the enzyme in the extracellular space
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N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
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NAAG peptidase inhibitor reduces acute neuronal degeneration and astrocyte damage following lateral fluid percussion TBI in rats
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N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
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supply of the primary excitatory neurotransmitter glutamate
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N-acetyl-alpha-L-aspartyl-L-glutamate + H2O
N-acetyl-alpha-L-aspartate + L-glutamate
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the enzyme is involved in glutamate-mediated neurodegenerative disorders, enzyme inhibition is a mechanism for reduction of excitotoxic glutamate
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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-Asp-Glu + H2O
N-acetyl-Asp + Glu
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N-acetyl-Asp-Glu + H2O
N-acetyl-Asp + Glu
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N-acetyl-Asp-Glu + H2O
N-acetyl-Asp + Glu
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the enzyme converts N-acetylaspartylglutamate from a neuroprotectant to a neurotoxin
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N-Acetyl-L-Asp-L-Glu + H2O
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functions as a cell surface peptidase, possibly hydrolzing peptides in prostatic fluid
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N-Acetyl-L-Asp-L-Glu + H2O
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may play a role in signaling between non-myelinating Schwann cells and peripheral axons
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N-Acetyl-L-Asp-L-Glu + H2O
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role in synaptic peptide degradation
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N-Acetyl-L-Asp-L-Glu + H2O
N-Acetyl-L-Asp + L-Glu
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N-Acetyl-L-Asp-L-Glu + H2O
N-Acetyl-L-Asp + L-Glu
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N-Acetyl-L-Asp-L-Glu + H2O
N-Acetyl-L-Asp + L-Glu
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N-Acetyl-L-Asp-L-Glu + H2O
N-Acetyl-L-Asp + L-Glu
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N-Acetyl-L-Asp-L-Glu + H2O
N-Acetyl-L-Asp + L-Glu
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N-Acetyl-L-Asp-L-Glu + H2O
N-Acetyl-L-Asp + L-Glu
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N-Acetyl-L-Asp-L-Glu + H2O
N-Acetyl-L-Asp + L-Glu
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no formation of acetate
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N-acetyl-L-aspartyl-L-glutamate + H2O
L-glutamate + N-acetyl-L-aspartate
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N-acetyl-L-aspartyl-L-glutamate + H2O
L-glutamate + N-acetyl-L-aspartate
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NAALADase, a neuropeptidase that produces the neurotransmitter glutamate and N-acetyl-Laspartate throught hydrolysis of N-acetyl-L-aspartyl-L-glutamate
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N-acetyl-L-aspartyl-L-glutamate + H2O
L-glutamate + N-acetyl-L-aspartate
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N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-Asp + L-Glu
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N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-Asp + L-Glu
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N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
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N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
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N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
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N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
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N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
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N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
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N-acetyl-L-aspartyl-L-glutamate + H2O
N-acetyl-L-aspartate + L-glutamate
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poly-gamma-glutamate folate + H2O
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poly-gamma-glutamate folate + H2O
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activity outside of the cell
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poly-gamma-glutamate folate + H2O
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poly-gamma-glutamate folate + H2O
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activity outside of the cell
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pteroyl-di-L-glutamate + H2O
L-Glu + pteroylglutamate
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pteroyl-di-L-glutamate + H2O
L-Glu + pteroylglutamate
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additional information
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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
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additional information
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the enzyme interacts with filamin leading to internalization of PMSA into cells in the perinuclear region, overview
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additional information
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bifunctional enzyme performing folate hydrolase and N-acetylated alpha-linked acidic dipeptidase, NAALADase, activities
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additional information
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bifunctional enzyme performing folate hydrolase and N-acetylated alpha-linked acidic dipeptidase, NAALADase, activities
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additional information
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bifunctional enzyme performing folate hydrolase and N-acetylated alpha-linked acidic dipeptidase, NAALADase, activities
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additional information
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intestinal absorption of polyglutamyl folates involves cleavage of the glutamate side chain by FGCP
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additional information
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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
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additional information
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PSMA is highly homologous to N-acetylated alpha-linked acidic dipeptidase, NAALADase
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additional information
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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
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additional information
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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
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additional information
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no substrate: amyloid-beta
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additional information
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no substrate: amyloid-beta
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additional information
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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
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additional information
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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
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additional information
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no cleavage of beta-citrylglutamate
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additional information
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no cleavage of beta-citrylglutamate
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additional information
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the enzyme interacts with filamin leading to internalization of PMSA into cells in the perinuclear region, overview
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additional information
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bifunctional enzyme performing folate hydrolase and N-acetylated alpha-linked acidic dipeptidase, NAALADase, activities
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additional information
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mouse glutamate carboxypeptidase II possesses lower catalytic efficiency but similar substrate specificity compared with the human protein
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additional information
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mouse glutamate carboxypeptidase II possesses lower catalytic efficiency but similar substrate specificity compared with the human protein
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additional information
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enzyme inhibition depresses mossy fiber-CA3 synaptic transmission
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