PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19887726-3	2009	In the assay of AGT activity using crude enzyme preparations, there is the complication that glutamate:glyoxylate aminotransferase (GGT) also contributes to AGT activity, but at present no other enzyme is known to catalyze transamination between L-serine and glyoxylate or pyruvate.	Glutamic Acid	93-102	alanine--glyoxylate and serine--pyruvate aminotransferase	Homo sapiens	16-19	
19887726-3	2009	In the assay of AGT activity using crude enzyme preparations, there is the complication that glutamate:glyoxylate aminotransferase (GGT) also contributes to AGT activity, but at present no other enzyme is known to catalyze transamination between L-serine and glyoxylate or pyruvate.	Glutamic Acid	93-102	alanine--glyoxylate and serine--pyruvate aminotransferase	Homo sapiens	157-160	
1349575-0	1992	A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1.	Glutamic Acid	13-22	alanine--glyoxylate and serine--pyruvate aminotransferase	Homo sapiens	46-81	
3416563-7	1988	When corrected for cross-over from glutamate:glyoxylate aminotransferase (GGT; EC 2.6.1.4), the mean AGT activity in the PH1 livers was reduced to 3.3% of the control values.	Glutamic Acid	35-44	alanine--glyoxylate and serine--pyruvate aminotransferase	Homo sapiens	121-124