PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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-ammonia ligase Homo sapiens 59-82 24927554-1 2014 The human neuroendocrine enzyme glutamate decarboxylase (GAD) catalyses the synthesis of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) using pyridoxal 5"-phosphate as a cofactor. Pyridoxal Phosphate 158-180 glutamate-ammonia ligase Homo sapiens 32-55 24927554-1 2014 The human neuroendocrine enzyme glutamate decarboxylase (GAD) catalyses the synthesis of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) using pyridoxal 5"-phosphate as a cofactor. Pyridoxal Phosphate 158-180 glutamate-ammonia ligase Homo sapiens 57-60 12887686-2 2003 GAD activity is regulated by a cycle of activation and inactivation determined by the binding and release of its co-factor, pyridoxal 5"-phosphate. Pyridoxal Phosphate 124-146 glutamate-ammonia ligase Homo sapiens 0-3 10190974-0 1999 Conformational alteration in serum albumin as a carrier for pyridoxal phosphate: a distinction from pyridoxal phosphate-dependent glutamate decarboxylase. Pyridoxal Phosphate 100-119 glutamate-ammonia ligase Homo sapiens 130-153 10190974-7 1999 To help in understanding BSA as a carrier for pyridoxal-P, the results were compared with those for glutamate decarboxylase (GAD), a pyridoxal-P-dependent protein, which requires pyridoxal-P as the cofactor for activity. Pyridoxal Phosphate 133-144 glutamate-ammonia ligase Homo sapiens 125-128 10190974-8 1999 Although BSA and GAD exhibit comparable molecular weights (66430 versus 65300), numbers of amino acid residues (582 versus 585), and binding affinity (>10(6) M-1), distinct conformational alterations occur between the two proteins upon interacting with pyridoxal-P: a small conformational change for BSA versus a large conformational change for GAD. Pyridoxal Phosphate 256-267 glutamate-ammonia ligase Homo sapiens 17-20 12535612-1 2003 The interactions between glutamate decarboxylase (GAD) and its cofactor pyridoxal phosphate (PLP) play a key role in the regulation of GAD activity. Pyridoxal Phosphate 72-91 glutamate-ammonia ligase Homo sapiens 25-48 12535612-1 2003 The interactions between glutamate decarboxylase (GAD) and its cofactor pyridoxal phosphate (PLP) play a key role in the regulation of GAD activity. Pyridoxal Phosphate 72-91 glutamate-ammonia ligase Homo sapiens 50-53 12535612-1 2003 The interactions between glutamate decarboxylase (GAD) and its cofactor pyridoxal phosphate (PLP) play a key role in the regulation of GAD activity. Pyridoxal Phosphate 72-91 glutamate-ammonia ligase Homo sapiens 135-138 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-ammonia ligase Homo sapiens 59-82 7885536-1 1994 Pyridoxine-dependent seizures are a disorder of GABA metabolism probably due to a defective binding of pyridoxal phosphate coenzyme (PALP) with glutamate decarboxylase (GAD), the rate-limiting enzyme in GABA synthesis. Pyridoxal Phosphate 103-122 glutamate-ammonia ligase Homo sapiens 144-167 9621518-2 1998 The defect has been suggested to reside in glutamate decarboxylase (GAD), since a mutant GAD with an abnormally high Km for a cofactor, pyridoxal phosphate, could not synthesize an adequate amount of gamma-amino butyric acid [Scriver and Whelan (1969) Ann NY Acad Sci 166: 83]. Pyridoxal Phosphate 136-155 glutamate-ammonia ligase Homo sapiens 43-66 9621518-2 1998 The defect has been suggested to reside in glutamate decarboxylase (GAD), since a mutant GAD with an abnormally high Km for a cofactor, pyridoxal phosphate, could not synthesize an adequate amount of gamma-amino butyric acid [Scriver and Whelan (1969) Ann NY Acad Sci 166: 83]. Pyridoxal Phosphate 136-155 glutamate-ammonia ligase Homo sapiens 68-71 9621518-2 1998 The defect has been suggested to reside in glutamate decarboxylase (GAD), since a mutant GAD with an abnormally high Km for a cofactor, pyridoxal phosphate, could not synthesize an adequate amount of gamma-amino butyric acid [Scriver and Whelan (1969) Ann NY Acad Sci 166: 83]. Pyridoxal Phosphate 136-155 glutamate-ammonia ligase Homo sapiens 89-92 7567987-6 1995 Interestingly, pyridoxal phosphate is the cofactor of both aromatic L-amino acid decarboxylase and glutamate decarboxylase. Pyridoxal Phosphate 15-34 glutamate-ammonia ligase Homo sapiens 99-122 7885536-1 1994 Pyridoxine-dependent seizures are a disorder of GABA metabolism probably due to a defective binding of pyridoxal phosphate coenzyme (PALP) with glutamate decarboxylase (GAD), the rate-limiting enzyme in GABA synthesis. Pyridoxal Phosphate 103-122 glutamate-ammonia ligase Homo sapiens 169-172 2878977-1 1987 In the absence of its cofactor, pyridoxal 5"-phosphate (pyridoxal-P), glutamate decarboxylase is rapidly inactivated by aspartate. Pyridoxal Phosphate 32-54 glutamate-ammonia ligase Homo sapiens 70-93 8419527-5 1993 The interaction of GAD with pyridoxal-P is a major factor in the short-term regulation of GAD activity. Pyridoxal Phosphate 28-39 glutamate-ammonia ligase Homo sapiens 19-22 8419527-5 1993 The interaction of GAD with pyridoxal-P is a major factor in the short-term regulation of GAD activity. Pyridoxal Phosphate 28-39 glutamate-ammonia ligase Homo sapiens 90-93 2574957-0 1989 A microassay for the determination of soluble and membrane-bound glutamate decarboxylase activity--influences of cations, lipid composition, and pyridoxal 5"-phosphate on the glutamate decarboxylase binding to liposomes. Pyridoxal Phosphate 145-167 glutamate-ammonia ligase Homo sapiens 175-198 1637919-0 1992 [Reactivation and reconstitution of glutamate decarboxylase upon the interaction of its dimers with pyridoxal phosphate]. Pyridoxal Phosphate 100-119 glutamate-ammonia ligase Homo sapiens 36-59 1637919-1 1992 The relationship between the reactivation and reconstitution of the hexameric form of glutamate decarboxylase during the interaction of inactive apoenzyme dimers with pyridoxal phosphate (PLP) has been studied. Pyridoxal Phosphate 167-186 glutamate-ammonia ligase Homo sapiens 86-109 1637919-1 1992 The relationship between the reactivation and reconstitution of the hexameric form of glutamate decarboxylase during the interaction of inactive apoenzyme dimers with pyridoxal phosphate (PLP) has been studied. Pyridoxal Phosphate 188-191 glutamate-ammonia ligase Homo sapiens 86-109 2069576-1 1991 We have recorded 1H NMR spectra in H2O for exchangeable protons of four pyridoxal phosphate-dependent enzymes: D-serine dehydratase, aspartate aminotransferase, tryptophan: indole-lyase and glutamate decarboxylase. Pyridoxal Phosphate 72-91 glutamate-ammonia ligase Homo sapiens 190-213 2069816-3 1991 The brain contains two forms of the GABA synthetic enzyme glutamate decarboxylase (GAD), which differ in molecular size, amino acid sequence, antigenicity, cellular and subcellular location, and interaction with the GAD cofactor pyridoxal phosphate. Pyridoxal Phosphate 229-248 glutamate-ammonia ligase Homo sapiens 58-81 2069816-3 1991 The brain contains two forms of the GABA synthetic enzyme glutamate decarboxylase (GAD), which differ in molecular size, amino acid sequence, antigenicity, cellular and subcellular location, and interaction with the GAD cofactor pyridoxal phosphate. Pyridoxal Phosphate 229-248 glutamate-ammonia ligase Homo sapiens 83-86 2069816-3 1991 The brain contains two forms of the GABA synthetic enzyme glutamate decarboxylase (GAD), which differ in molecular size, amino acid sequence, antigenicity, cellular and subcellular location, and interaction with the GAD cofactor pyridoxal phosphate. Pyridoxal Phosphate 229-248 glutamate-ammonia ligase Homo sapiens 216-219 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-ammonia ligase Homo sapiens 95-118 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-ammonia ligase Homo sapiens 95-118 3326683-5 1987 The interaction of glutamate decarboxylase with its cofactor, pyridoxal 5"-phosphate, is a regulated process and appears to be one of the major means of controlling enzyme activity. Pyridoxal Phosphate 62-84 glutamate-ammonia ligase Homo sapiens 19-42 2878977-1 1987 In the absence of its cofactor, pyridoxal 5"-phosphate (pyridoxal-P), glutamate decarboxylase is rapidly inactivated by aspartate. Pyridoxal Phosphate 56-67 glutamate-ammonia ligase Homo sapiens 70-93 32041144-1 2020 Glutamate decarboxylase (GAD; EC 4.1.1.15) is a unique pyridoxal 5-phosphate (PLP)-dependent enzyme that specifically catalyzes the decarboxylation of L-glutamic acid to produce gamma-aminobutyric acid (GABA), which exhibits several well-known physiological functions. Pyridoxal Phosphate 55-76 glutamate-ammonia ligase Homo sapiens 0-23 5160156-0 1971 A proposed structure for the 330 -nm chromophore of glutamate decarboxylase and other pyridoxal 5"-phosphate dependent enzymes. Pyridoxal Phosphate 87-109 glutamate-ammonia ligase Homo sapiens 53-76 5542022-0 1971 Kinetics of the binding of pyridoxal 5"-phosphate to glutamate decarboxylase. Pyridoxal Phosphate 27-49 glutamate-ammonia ligase Homo sapiens 53-76 5511287-0 1970 Protective effect of pyridoxal-5-phosphate on glutamate decarboxylase from lupin seeds. Pyridoxal Phosphate 21-42 glutamate-ammonia ligase Homo sapiens 46-69 6136327-11 1983 Glutamate-promoted inactivation, its enhancement by ATP, and the opposition to inactivation by pyridoxal-P and Pi appear to be important in the regulation of glutamate decarboxylase. Pyridoxal Phosphate 95-106 glutamate-ammonia ligase Homo sapiens 158-181 6136328-9 1983 Four factors (glutamate, pyridoxal-P, ATP, and Pi) control a cycle of inactivation and reactivation that appears to be important in the regulation of brain glutamate decarboxylase. Pyridoxal Phosphate 25-36 glutamate-ammonia ligase Homo sapiens 156-179 5780984-0 1969 Effects of various substituted hydrazones and hydrazines of pyridoxal-5"-phosphate on brain glutamate decarboxylase. Pyridoxal Phosphate 60-82 glutamate-ammonia ligase Homo sapiens 92-115 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-ammonia ligase Homo sapiens 0-23 32041144-1 2020 Glutamate decarboxylase (GAD; EC 4.1.1.15) is a unique pyridoxal 5-phosphate (PLP)-dependent enzyme that specifically catalyzes the decarboxylation of L-glutamic acid to produce gamma-aminobutyric acid (GABA), which exhibits several well-known physiological functions. Pyridoxal Phosphate 55-76 glutamate-ammonia ligase Homo sapiens 25-28 32041144-1 2020 Glutamate decarboxylase (GAD; EC 4.1.1.15) is a unique pyridoxal 5-phosphate (PLP)-dependent enzyme that specifically catalyzes the decarboxylation of L-glutamic acid to produce gamma-aminobutyric acid (GABA), which exhibits several well-known physiological functions. Pyridoxal Phosphate 78-81 glutamate-ammonia ligase Homo sapiens 0-23 32041144-1 2020 Glutamate decarboxylase (GAD; EC 4.1.1.15) is a unique pyridoxal 5-phosphate (PLP)-dependent enzyme that specifically catalyzes the decarboxylation of L-glutamic acid to produce gamma-aminobutyric acid (GABA), which exhibits several well-known physiological functions. Pyridoxal Phosphate 78-81 glutamate-ammonia ligase Homo sapiens 25-28