PMID-sentid Pub_year Sent_text compound_name comp_offset prot_official_name organism prot_offset 3346674-1 1988 N-Acetylated-alpha-linked acidic dipeptidase (NAALADase) is a Cl- dependent, membrane bound, metallopeptidase that cleaves the endogenous neuropeptide N-acetyl-L-aspartyl-L-glutamate (NAAG) in vitro. Ac-Asp-Glu(3-) 151-182 folate hydrolase 1B (pseudogene) Homo sapiens 0-44 34684866-1 2021 We report the results of a computational study of the hydrolysis reaction mechanism of N-acetyl-l-aspartyl-l-glutamate (NAAG) catalyzed by glutamate carboxypeptidase II. Ac-Asp-Glu(3-) 87-118 folate hydrolase 1 Homo sapiens 139-168 3346674-1 1988 N-Acetylated-alpha-linked acidic dipeptidase (NAALADase) is a Cl- dependent, membrane bound, metallopeptidase that cleaves the endogenous neuropeptide N-acetyl-L-aspartyl-L-glutamate (NAAG) in vitro. Ac-Asp-Glu(3-) 151-182 folate hydrolase 1B (pseudogene) Homo sapiens 46-55 27589333-3 2016 Radiolabeled peptide targeting technologies have rapidly evolved over the last decade and have focused on the successful development of radiolabeled small molecules that act as inhibitors to the binding of the N-acetyl-l-aspartyl-l-glutamate (NAAG) substrate to the PSMA molecule. Ac-Asp-Glu(3-) 210-241 folate hydrolase 1 Homo sapiens 266-270 3667587-2 1987 High performance liquid chromatography studies documented the presence of an enzyme activity, N-acetylated alpha-linked acidic dipeptidase (NAALA dipeptidase), in rat brain membranes that cleaves the endogenous brain dipeptide, N-acetyl-L-aspartyl-L-glutamate to N-acetyl-aspartate and glutamate. Ac-Asp-Glu(3-) 228-259 folate hydrolase 1 Rattus norvegicus 94-138 24647901-1 2014 BACKGROUND: Glutamate carboxypeptidase II (GCPII) is a transmembrane enzyme that cleaves N-acetyl-L-aspartyl-L-glutamate (NAAG) in the brain. Ac-Asp-Glu(3-) 89-120 folate hydrolase 1 Homo sapiens 12-41 24647901-1 2014 BACKGROUND: Glutamate carboxypeptidase II (GCPII) is a transmembrane enzyme that cleaves N-acetyl-L-aspartyl-L-glutamate (NAAG) in the brain. Ac-Asp-Glu(3-) 89-120 folate hydrolase 1 Homo sapiens 43-48 17714508-3 2007 To complement and extend the structural studies, we constructed a model of GCPII in complex with its substrate, N-acetyl-l-aspartyl-l-glutamate, which enabled us to predict additional amino acid residues interacting with the bound substrate, and used site-directed mutagenesis to assess the contribution of individual residues for substrate/inhibitor binding and enzymatic activity of GCPII. Ac-Asp-Glu(3-) 112-143 folate hydrolase 1 Homo sapiens 75-80 23891752-1 2013 We recently reported that glutamate carboxypeptidase II (GCPII) has a new physiological function degrading amyloid-beta (Abeta), distinct from its own hydrolysis activity in N-acetyl-L-aspartyl-L-glutamate (NAAG); however, its underlying mechanism remains undiscovered. Ac-Asp-Glu(3-) 174-205 folate hydrolase 1 Homo sapiens 26-55 23891752-1 2013 We recently reported that glutamate carboxypeptidase II (GCPII) has a new physiological function degrading amyloid-beta (Abeta), distinct from its own hydrolysis activity in N-acetyl-L-aspartyl-L-glutamate (NAAG); however, its underlying mechanism remains undiscovered. Ac-Asp-Glu(3-) 174-205 folate hydrolase 1 Homo sapiens 57-62 23525279-5 2013 GCPII is a zinc exopeptidase that cleaves glutamate from N-acetyl-L-aspartyl-L-glutamate in the central nervous system and from pteroylpoly-gamma-glutamate in the jejunum. Ac-Asp-Glu(3-) 57-88 folate hydrolase 1 Homo sapiens 0-5 19301871-2 2009 The hydrolysis of N-acetyl-l-aspartyl-l-glutamate (N-Ac-Asp-Glu), the natural dipeptidic substrate of the GCPII, is intimately involved in cellular signaling within the mammalian nervous system, but the exact mechanism of this reaction has not yet been determined. Ac-Asp-Glu(3-) 18-49 folate hydrolase 1 Homo sapiens 106-111 17714508-3 2007 To complement and extend the structural studies, we constructed a model of GCPII in complex with its substrate, N-acetyl-l-aspartyl-l-glutamate, which enabled us to predict additional amino acid residues interacting with the bound substrate, and used site-directed mutagenesis to assess the contribution of individual residues for substrate/inhibitor binding and enzymatic activity of GCPII. Ac-Asp-Glu(3-) 112-143 folate hydrolase 1 Homo sapiens 385-390 16467855-1 2006 Membrane-bound glutamate carboxypeptidase II (GCPII) is a zinc metalloenzyme that catalyzes the hydrolysis of the neurotransmitter N-acetyl-L-aspartyl-L-glutamate (NAAG) to N-acetyl-L-aspartate and L-glutamate (which is itself a neurotransmitter). Ac-Asp-Glu(3-) 131-162 folate hydrolase 1 Homo sapiens 15-44 16467855-1 2006 Membrane-bound glutamate carboxypeptidase II (GCPII) is a zinc metalloenzyme that catalyzes the hydrolysis of the neurotransmitter N-acetyl-L-aspartyl-L-glutamate (NAAG) to N-acetyl-L-aspartate and L-glutamate (which is itself a neurotransmitter). Ac-Asp-Glu(3-) 131-162 folate hydrolase 1 Homo sapiens 46-51 15152093-2 2004 The GCPII form expressed in the central nervous system, termed NAALADase, is responsible for the cleavage of N-acetyl-L-aspartyl-L-glutamate (NAAG) yielding free glutamate in the synaptic cleft, and is implicated in various pathologic conditions associated with glutamate excitotoxicity. Ac-Asp-Glu(3-) 109-140 folate hydrolase 1 Homo sapiens 4-9 15837926-2 2005 PSMA acts as a glutamate carboxypeptidase (GCPII) on small molecule substrates, including folate, the anticancer drug methotrexate, and the neuropeptide N-acetyl-l-aspartyl-l-glutamate. Ac-Asp-Glu(3-) 153-184 folate hydrolase 1 Homo sapiens 0-4 15837926-2 2005 PSMA acts as a glutamate carboxypeptidase (GCPII) on small molecule substrates, including folate, the anticancer drug methotrexate, and the neuropeptide N-acetyl-l-aspartyl-l-glutamate. Ac-Asp-Glu(3-) 153-184 folate hydrolase 1 Homo sapiens 43-48 15837926-5 2005 Elucidation of the PSMA structure combined with docking studies and a proposed catalytic mechanism provides insight into the recognition of inhibitors and the natural substrate N-acetyl-l-aspartyl-l-glutamate. Ac-Asp-Glu(3-) 177-208 folate hydrolase 1 Homo sapiens 19-23 15152093-2 2004 The GCPII form expressed in the central nervous system, termed NAALADase, is responsible for the cleavage of N-acetyl-L-aspartyl-L-glutamate (NAAG) yielding free glutamate in the synaptic cleft, and is implicated in various pathologic conditions associated with glutamate excitotoxicity. Ac-Asp-Glu(3-) 109-140 folate hydrolase 1 Homo sapiens 63-72 11755246-1 2002 Intracerebroventricular administration of N-acetyl-L-aspartyl-L-glutamate (NAAG), an agonist at group II metabotropic and NR1/NR2D-containing N-methyl-D-aspartate (NMDA) ionotropic glutamate receptors, increased the permeability of the blood-brain barrier (BBB) to serum albumin in the striatum, but produced no similar effects in the entorhinal cortex or in the hippocampal formation. Ac-Asp-Glu(3-) 42-73 glutamate ionotropic receptor NMDA type subunit 1 Rattus norvegicus 122-125 15027864-1 2004 The neuropeptidase glutamate carboxypeptidase II (GCPII) hydrolyzes N-acetyl-L-aspartyl-L-glutamate (NAAG) to liberate N-acetylaspartate and glutamate. Ac-Asp-Glu(3-) 68-99 folate hydrolase 1 Homo sapiens 19-48 15027864-1 2004 The neuropeptidase glutamate carboxypeptidase II (GCPII) hydrolyzes N-acetyl-L-aspartyl-L-glutamate (NAAG) to liberate N-acetylaspartate and glutamate. Ac-Asp-Glu(3-) 68-99 folate hydrolase 1 Homo sapiens 50-55 11755246-1 2002 Intracerebroventricular administration of N-acetyl-L-aspartyl-L-glutamate (NAAG), an agonist at group II metabotropic and NR1/NR2D-containing N-methyl-D-aspartate (NMDA) ionotropic glutamate receptors, increased the permeability of the blood-brain barrier (BBB) to serum albumin in the striatum, but produced no similar effects in the entorhinal cortex or in the hippocampal formation. Ac-Asp-Glu(3-) 42-73 glutamate ionotropic receptor NMDA type subunit 2D Rattus norvegicus 126-130 9501243-1 1998 N-acetylated alpha-linked acidic dipeptidase (NAALADase) hydrolyzes acidic peptides, such as the abundant neuropeptide N-acetyl-alpha-L-aspartyl-L-glutamate (NAAG), thereby generating glutamate. Ac-Asp-Glu(3-) 119-156 folate hydrolase 1 Rattus norvegicus 0-44 10085079-1 1999 Hydrolysis of the neuropeptide N-acetyl-L-aspartyl-L-glutamate (NAAG) by N-acetylated alpha-linked acidic dipeptidase (NAALADase) to release glutamate may be important in a number of neurodegenerative disorders in which excitotoxic mechanisms are implicated. Ac-Asp-Glu(3-) 31-62 folate hydrolase 1B (pseudogene) Homo sapiens 73-117 10085079-1 1999 Hydrolysis of the neuropeptide N-acetyl-L-aspartyl-L-glutamate (NAAG) by N-acetylated alpha-linked acidic dipeptidase (NAALADase) to release glutamate may be important in a number of neurodegenerative disorders in which excitotoxic mechanisms are implicated. Ac-Asp-Glu(3-) 31-62 folate hydrolase 1B (pseudogene) Homo sapiens 119-128 9755050-2 1998 In the present study we characterize the transport function of the rat brain PEPT2, with special emphasis on electrophysiological properties and interaction with N-acetyl-L-aspartyl-L-glutamate (NAAG). Ac-Asp-Glu(3-) 162-193 solute carrier family 15 member 2 L homeolog Xenopus laevis 77-82 9501243-1 1998 N-acetylated alpha-linked acidic dipeptidase (NAALADase) hydrolyzes acidic peptides, such as the abundant neuropeptide N-acetyl-alpha-L-aspartyl-L-glutamate (NAAG), thereby generating glutamate. Ac-Asp-Glu(3-) 119-156 folate hydrolase 1 Rattus norvegicus 46-55 2250024-2 1990 N-Acetylated alpha-linked acidic dipeptidase (NAALA dipeptidase) is a membrane-bound metallopeptidase that cleaves glutamate from the endogenous neuropeptide N-acetyl-L-aspartyl-L-glutamate. Ac-Asp-Glu(3-) 158-189 folate hydrolase 1 Rattus norvegicus 0-44 1944768-6 1991 The regional distribution of brain NAG differs from that of NAA and resembles that of N-acetyl-L-aspartyl-L-glutamate (NAAG), suggesting that NAG and NAAG are related. Ac-Asp-Glu(3-) 86-117 neuroblastoma amplified sequence Gallus gallus 35-38