PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29110180-2 2018 AGT prevents oxalate formation by converting peroxisomal glyoxylate to glycine. Glycine 71-78 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 0-3 7798168-10 1994 111, 2341-2351 (1990)] have reported that Pro-11, Gly-170, and Ile-340 in normal human AGT1 were replaced by Leu, Arg, and Met, respectively, in a patient with primary hyperoxaluria type 1. Glycine 50-53 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 87-91 1349575-0 1992 A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1. Glycine 2-9 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 46-81 11330044-1 2000 Glyoxylate is an immediate precursor of oxalate, but in its metabolism the conversion into glycine catalyzed by serine:pyruvate/alanine:glyoxylate aminotransferase (SPT/AGT) appears to be the main route. Glycine 91-98 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 165-168 35625596-3 2022 By enriching LCSCs from spheroid cultures and performing transcriptomic analysis, we determined that alanine-glyoxylate aminotransferase (AGXT), which participates in the metabolism of serine and glycine, was significantly upregulated in spheroid cultures, and its function in LCSCs remains unknown. Glycine 196-203 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 101-136 35625596-3 2022 By enriching LCSCs from spheroid cultures and performing transcriptomic analysis, we determined that alanine-glyoxylate aminotransferase (AGXT), which participates in the metabolism of serine and glycine, was significantly upregulated in spheroid cultures, and its function in LCSCs remains unknown. Glycine 196-203 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 138-142 3302715-2 1987 The main catabolic pathway of nutritional glycine proceeds via the glycine-cleavage enzyme, serinehydroxymethyltransferase and serinedehydratase or serine-pyruvate aminotransferase and via serine and pyruvate. Glycine 42-49 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 148-180 25620715-1 2015 Liver peroxisomal alanine:glyoxylate aminotransferase (AGT) (EC 2.6.1.44) catalyses the conversion of l-alanine and glyoxylate to pyruvate and glycine, a reaction that allows glyoxylate detoxification. Glycine 143-150 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 18-53 20301460-0 1993 Primary Hyperoxaluria Type 1 CLINICAL CHARACTERISTICS: Primary hyperoxaluria type 1 (PH1) is caused by a deficiency of the liver peroxisomal enzyme alanine:glyoxylate-aminotransferase (AGT), which catalyzes the conversion of glyoxylate to glycine. Glycine 239-246 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 85-88 20301460-0 1993 Primary Hyperoxaluria Type 1 CLINICAL CHARACTERISTICS: Primary hyperoxaluria type 1 (PH1) is caused by a deficiency of the liver peroxisomal enzyme alanine:glyoxylate-aminotransferase (AGT), which catalyzes the conversion of glyoxylate to glycine. Glycine 239-246 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 148-183 28916765-1 2017 The alanine:glyoxylate aminotransferase (AGT), a hepatocyte-specific pyridoxal-5"-phosphate (PLP) dependent enzyme, transaminates L-alanine and glyoxylate to glycine and pyruvate, thus detoxifying glyoxylate and preventing pathological oxalate precipitation in tissues. Glycine 158-165 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 4-39 28916765-1 2017 The alanine:glyoxylate aminotransferase (AGT), a hepatocyte-specific pyridoxal-5"-phosphate (PLP) dependent enzyme, transaminates L-alanine and glyoxylate to glycine and pyruvate, thus detoxifying glyoxylate and preventing pathological oxalate precipitation in tissues. Glycine 158-165 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 41-44 26854734-8 2016 These data support the suggestion that the effectiveness of pharmacological doses of pyridoxine results from an improved metabolic effectiveness of AGT; that is the increased rate of transamination of glyoxylate to glycine. Glycine 215-222 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 148-151 25620715-1 2015 Liver peroxisomal alanine:glyoxylate aminotransferase (AGT) (EC 2.6.1.44) catalyses the conversion of l-alanine and glyoxylate to pyruvate and glycine, a reaction that allows glyoxylate detoxification. Glycine 143-150 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 55-58 23956997-1 2013 Alanine-glyoxylate aminotransferase catalyzes the transamination between L-alanine and glyoxylate to produce pyruvate and glycine using pyridoxal 5"-phosphate (PLP) as cofactor. Glycine 122-129 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 0-35 22446032-4 2012 Alanine-glyoxylate aminotransferase, a peroxisomal enzyme in humans, converts glyoxylate into glycine, playing a central role in glyoxylate detoxification. Glycine 94-101 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 0-35 19155213-1 2009 Human liver peroxisomal alanine:glyoxylate aminotransferase (AGT) is a pyridoxal 5"-phosphate (PLP)-dependent enzyme that converts glyoxylate into glycine. Glycine 147-154 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 24-59 20133649-0 2010 Molecular defects of the glycine 41 variants of alanine glyoxylate aminotransferase associated with primary hyperoxaluria type I. Glycine 25-32 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 48-83 19545238-1 2009 PH1 (primary hyperoxaluria type 1) is a severe inborn disorder of glyoxylate metabolism caused by a functional deficiency of the peroxisomal enzyme AGXT (alanine-glyoxylate aminotransferase), which converts glyoxylate into glycine using L-alanine as the amino-group donor. Glycine 223-230 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 0-3 19545238-1 2009 PH1 (primary hyperoxaluria type 1) is a severe inborn disorder of glyoxylate metabolism caused by a functional deficiency of the peroxisomal enzyme AGXT (alanine-glyoxylate aminotransferase), which converts glyoxylate into glycine using L-alanine as the amino-group donor. Glycine 223-230 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 5-33 19545238-1 2009 PH1 (primary hyperoxaluria type 1) is a severe inborn disorder of glyoxylate metabolism caused by a functional deficiency of the peroxisomal enzyme AGXT (alanine-glyoxylate aminotransferase), which converts glyoxylate into glycine using L-alanine as the amino-group donor. Glycine 223-230 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 154-189 19155213-1 2009 Human liver peroxisomal alanine:glyoxylate aminotransferase (AGT) is a pyridoxal 5"-phosphate (PLP)-dependent enzyme that converts glyoxylate into glycine. Glycine 147-154 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 61-64 18289107-3 2008 Alanine:glyoxylate aminotransferase (AGT) is a peroxisomal pyridoxal 5"-phosphate (PLP) dependent enzyme which catalyzes the transamination of alanine and glyoxylate to pyruvate and glycine. Glycine 182-189 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 0-35 18289107-3 2008 Alanine:glyoxylate aminotransferase (AGT) is a peroxisomal pyridoxal 5"-phosphate (PLP) dependent enzyme which catalyzes the transamination of alanine and glyoxylate to pyruvate and glycine. Glycine 182-189 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 37-40 16970975-2 2007 Once formed, the molecule can be converted to glycine by alanine-glyoxylate aminotransferase (AGAT). Glycine 46-53 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 57-92 15240345-10 2004 Mitochondria, which produce glyoxylate from hydroxyproline metabolism, contained both alanine:glyoxylate aminotransferase (AGT)2 and glyoxylate reductase activities, which can convert glyoxylate to glycine and glycolate, respectively. Glycine 198-205 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 86-121 15464418-2 2004 The disease is caused by a deficiency of alanine:glyoxylate aminotransferase (AGT) which catalyzes the conversion of glyoxylate to glycine. Glycine 131-138 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 41-76 15464418-2 2004 The disease is caused by a deficiency of alanine:glyoxylate aminotransferase (AGT) which catalyzes the conversion of glyoxylate to glycine. Glycine 131-138 alanine--glyoxylate and serine--pyruvate aminotransferase Homo sapiens 78-81