PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10978228-2 2000 The pathogenesis of PDE is unknown, but an alteration in the binding of pyridoxal 5-phosphate to glutamic acid decarboxylase (GAD) has been postulated in patients with PDE. Pyridoxal Phosphate 72-93 glutamate decarboxylase 1 Homo sapiens 97-124 12067524-5 2002 METHODS: Studies were performed on enzymatic activity of rGAD67/65 by production of 3H-GABA from 3H-glutamate, enzyme kinetics, binding to the enzyme cofactor pyridoxal phosphate (PLP), stability according to differences in pH, temperature and duration of storage, and antigenic reactivity with various GAD-specific antisera. Pyridoxal Phosphate 159-178 glutamate decarboxylase 1 Homo sapiens 58-61 10978228-2 2000 The pathogenesis of PDE is unknown, but an alteration in the binding of pyridoxal 5-phosphate to glutamic acid decarboxylase (GAD) has been postulated in patients with PDE. Pyridoxal Phosphate 72-93 glutamate decarboxylase 1 Homo sapiens 126-129 1988566-4 1991 In brain extracts, almost all GAD67 is in an active holoenzyme form, saturated with its cofactor, pyridoxal phosphate. Pyridoxal Phosphate 98-117 glutamate decarboxylase 1 Homo sapiens 30-35 7506741-7 1994 In one patient only, blocking was also observed by a peptide representing residues 390-402, which includes the binding site of the GAD cofactor, pyridoxal 5"-phosphate. Pyridoxal Phosphate 145-167 glutamate decarboxylase 1 Homo sapiens 131-134 8278600-6 1993 GAD65 is largely present as an inactive apoenzyme, which can be induced by nerve activity, while most GAD67 is present as a pyridoxal phosphate-bound permanently active holoenzyme. Pyridoxal Phosphate 124-143 glutamate decarboxylase 1 Homo sapiens 102-107 8419527-3 1993 Two forms, termed GAD65 and GAD67, are the products of two genes and differ in sequence, molecular weight, interaction with the cofactor, pyridoxal 5"-phosphate (pyridoxal-P), and level of expression among brain regions. Pyridoxal Phosphate 138-160 glutamate decarboxylase 1 Homo sapiens 28-33 8419527-3 1993 Two forms, termed GAD65 and GAD67, are the products of two genes and differ in sequence, molecular weight, interaction with the cofactor, pyridoxal 5"-phosphate (pyridoxal-P), and level of expression among brain regions. Pyridoxal Phosphate 162-173 glutamate decarboxylase 1 Homo sapiens 28-33 1956876-2 1991 With no pyridoxal-5-phosphate added, GAD was non-competitively inhibited by NaCN, with an IC50 of 280 microM. Pyridoxal Phosphate 8-29 glutamate decarboxylase 1 Homo sapiens 37-40 1956876-3 1991 GAD was also inhibited when exposed to an equimolar amount of NaCN and pyridoxal-5-phosphate. Pyridoxal Phosphate 71-92 glutamate decarboxylase 1 Homo sapiens 0-3 1956876-7 1991 The gamma-aminobutyric acid synthesizing enzyme, GAD may thus be inhibited in vivo by NaCN or by a reaction product of NaCN and pyridoxal-5-phosphate. Pyridoxal Phosphate 128-149 glutamate decarboxylase 1 Homo sapiens 49-52 9605314-1 1998 The pyridoxal-P binding sites of the two isoforms of human glutamate decarboxylase (GAD65 and GAD67) were modeled by using PROBE (a recently developed algorithm for multiple sequence alignment and database searching) to align the primary sequence of GAD with pyridoxal-P binding proteins of known structure. Pyridoxal Phosphate 4-15 glutamate decarboxylase 1 Homo sapiens 94-99 9605314-1 1998 The pyridoxal-P binding sites of the two isoforms of human glutamate decarboxylase (GAD65 and GAD67) were modeled by using PROBE (a recently developed algorithm for multiple sequence alignment and database searching) to align the primary sequence of GAD with pyridoxal-P binding proteins of known structure. Pyridoxal Phosphate 4-15 glutamate decarboxylase 1 Homo sapiens 84-87 9605314-1 1998 The pyridoxal-P binding sites of the two isoforms of human glutamate decarboxylase (GAD65 and GAD67) were modeled by using PROBE (a recently developed algorithm for multiple sequence alignment and database searching) to align the primary sequence of GAD with pyridoxal-P binding proteins of known structure. Pyridoxal Phosphate 259-270 glutamate decarboxylase 1 Homo sapiens 94-99 9605314-1 1998 The pyridoxal-P binding sites of the two isoforms of human glutamate decarboxylase (GAD65 and GAD67) were modeled by using PROBE (a recently developed algorithm for multiple sequence alignment and database searching) to align the primary sequence of GAD with pyridoxal-P binding proteins of known structure. Pyridoxal Phosphate 259-270 glutamate decarboxylase 1 Homo sapiens 84-87 9605314-7 1998 The key residues that interact directly with pyridoxal-P were identical in ornithine decarboxylase and the two GADs, thus allowing us to make a specific structural prediction of the cofactor binding site of GAD. Pyridoxal Phosphate 45-56 glutamate decarboxylase 1 Homo sapiens 111-114 23015103-1 2013 The production of gamma-aminobutyric acid (GABA) is catalyzed by two isoforms of glutamic acid decarboxylase (GAD), using pyridoxal 5"-phosphate (PLP) as the cofactor. Pyridoxal Phosphate 122-144 glutamate decarboxylase 1 Homo sapiens 81-108 35151785-3 2022 Several decarboxylases (aromatic amino acid decarboxylase, AADC; histidine decarboxylase, HDC; glutamate decarboxylase, GAD) catalyze the biosynthesis of neurotransmitters and neuromodulators and contain pyridoxal phosphate (PLP) as a cofactor. Pyridoxal Phosphate 204-223 glutamate decarboxylase 1 Homo sapiens 120-123 35151785-3 2022 Several decarboxylases (aromatic amino acid decarboxylase, AADC; histidine decarboxylase, HDC; glutamate decarboxylase, GAD) catalyze the biosynthesis of neurotransmitters and neuromodulators and contain pyridoxal phosphate (PLP) as a cofactor. Pyridoxal Phosphate 225-228 glutamate decarboxylase 1 Homo sapiens 120-123 6726228-5 1984 GAD was also eluted by its cofactor, pyridoxal 5"-phosphate, and this was enhanced by 1 mM Pi. Pyridoxal Phosphate 37-59 glutamate decarboxylase 1 Homo sapiens 0-3 33287375-1 2020 Glutamate decarboxylase (l-glutamate-1-carboxylase, GAD; EC 4.1.1.15) is a pyridoxal-5"-phosphate-dependent enzyme that catalyzes the irreversible alpha-decarboxylation of l-glutamic acid to gamma-aminobutyric acid (GABA) and CO2. Pyridoxal Phosphate 75-97 glutamate decarboxylase 1 Homo sapiens 52-55 23015103-1 2013 The production of gamma-aminobutyric acid (GABA) is catalyzed by two isoforms of glutamic acid decarboxylase (GAD), using pyridoxal 5"-phosphate (PLP) as the cofactor. Pyridoxal Phosphate 122-144 glutamate decarboxylase 1 Homo sapiens 110-113 23015103-1 2013 The production of gamma-aminobutyric acid (GABA) is catalyzed by two isoforms of glutamic acid decarboxylase (GAD), using pyridoxal 5"-phosphate (PLP) as the cofactor. Pyridoxal Phosphate 146-149 glutamate decarboxylase 1 Homo sapiens 81-108 23015103-1 2013 The production of gamma-aminobutyric acid (GABA) is catalyzed by two isoforms of glutamic acid decarboxylase (GAD), using pyridoxal 5"-phosphate (PLP) as the cofactor. Pyridoxal Phosphate 146-149 glutamate decarboxylase 1 Homo sapiens 110-113 15686475-3 2005 The activation appears to be due to an increase of GAD affinity for its cofactor, pyridoxal phosphate (PLP). Pyridoxal Phosphate 82-101 glutamate decarboxylase 1 Homo sapiens 51-54 17384644-1 2007 Gamma-aminobutyric acid (GABA) is synthesized by two isoforms of the pyridoxal 5"-phosphate-dependent enzyme glutamic acid decarboxylase (GAD65 and GAD67). Pyridoxal Phosphate 69-91 glutamate decarboxylase 1 Homo sapiens 148-153 16075246-2 2005 Although glutamate decarboxylase utilizes pyridoxal phosphate as a cofactor during conversion of the excitatory amino acid, glutamate, to the inhibitory neurotransmitter, gamma-amino butyric acid (GABA), several studies have failed to demonstrate a linkage to either of the glutamate-decarboxylase-encoding genes (GAD1 and GAD2) and PDS excluding involvement of this functional candidate. Pyridoxal Phosphate 42-61 glutamate decarboxylase 1 Homo sapiens 314-318 15070923-1 2004 The structurally related group II pyridoxal phosphate (PLP)-dependent amino acid decarboxylases glutamic acid decarboxylase (GAD), aromatic L-amino acid decarboxylase (AADC), and histidine decarboxylase (HDC) are known autoantigens in endocrine disorders. Pyridoxal Phosphate 34-53 glutamate decarboxylase 1 Homo sapiens 125-128 15381280-2 2004 GAD isoforms (GAD65 and GAD67) differ substantially in their interactions with cofactor pyridoxal 5"-phosphate, which is catalyzed by pyridoxal kinase (PLK). Pyridoxal Phosphate 88-110 glutamate decarboxylase 1 Homo sapiens 0-3 15381280-2 2004 GAD isoforms (GAD65 and GAD67) differ substantially in their interactions with cofactor pyridoxal 5"-phosphate, which is catalyzed by pyridoxal kinase (PLK). Pyridoxal Phosphate 88-110 glutamate decarboxylase 1 Homo sapiens 24-29