PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11950836-7	2002	Here we report the x-ray crystal structure of GlcAT-I in complex with the complete donor UDP-GlcUA, thereby providing structures of an inverting glycosyltransferase in which both the complete donor and acceptor substrates are present in the active site.	Uridine Diphosphate Glucuronic Acid	89-98	beta-1,3-glucuronyltransferase 3	Homo sapiens	46-53	
16815917-0	2006	Phylogenetic and mutational analyses reveal key residues for UDP-glucuronic acid binding and activity of beta1,3-glucuronosyltransferase I (GlcAT-I).	Uridine Diphosphate Glucuronic Acid	61-80	beta-1,3-glucuronyltransferase 3	Homo sapiens	140-147	
16300963-1	2006	The galactose-beta1,3-glucuronosyltransferase I (GlcAT-I) catalyzes the transfer of glucuronic acid from UDP-alpha-D-glucuronic acid onto the terminal galactose of the trisaccharide glycosaminoglycan-protein linker region of proteoglycans.	Uridine Diphosphate Glucuronic Acid	105-132	beta-1,3-glucuronyltransferase 3	Homo sapiens	4-47	
16300963-1	2006	The galactose-beta1,3-glucuronosyltransferase I (GlcAT-I) catalyzes the transfer of glucuronic acid from UDP-alpha-D-glucuronic acid onto the terminal galactose of the trisaccharide glycosaminoglycan-protein linker region of proteoglycans.	Uridine Diphosphate Glucuronic Acid	105-132	beta-1,3-glucuronyltransferase 3	Homo sapiens	49-56	
16815917-2	2006	Here, we develop phylogenetic and mutational approaches to identify critical residues involved in UDP-GlcA binding and enzyme activity of the human beta1,3-glucuronosyltransferase I (GlcAT-I), which plays a key role in glycosaminoglycan biosynthesis.	Uridine Diphosphate Glucuronic Acid	98-106	beta-1,3-glucuronyltransferase 3	Homo sapiens	183-190	
16815917-10	2006	Altogether, this phylogenetic approach sustained by biochemical analyses affords new insight into the organization of the beta1,3-glucuronosyltransferase family and distinguishes the respective importance of conserved residues in UDP-GlcA binding and activity of GlcAT-I.	Uridine Diphosphate Glucuronic Acid	230-238	beta-1,3-glucuronyltransferase 3	Homo sapiens	263-270	
11986319-2	2002	In this study, we identified His(308) and Arg(277) residues as essential determinants for the donor substrate (UDP-glucuronic acid) selectivity of the human GlcAT-I.	Uridine Diphosphate Glucuronic Acid	111-130	beta-1,3-glucuronyltransferase 3	Homo sapiens	157-164	
11986319-8	2002	Furthermore, the arginine-directed reagent 2,3-butanedione irreversibly inhibited GlcAT-I, which was effectively protected against inactivation by UDP-glucuronic acid but not by UDP-glucose.	Uridine Diphosphate Glucuronic Acid	147-166	beta-1,3-glucuronyltransferase 3	Homo sapiens	82-89	
10946001-3	2000	GlcAT-I transfers a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region trisaccharide Gal beta 1-3Gal beta 1-4Xyl covalently bound to a Ser residue at the glycosaminylglycan attachment site of proteoglycans.	Uridine Diphosphate Glucuronic Acid	52-87	beta-1,3-glucuronyltransferase 3	Homo sapiens	0-7	
10946001-3	2000	GlcAT-I transfers a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region trisaccharide Gal beta 1-3Gal beta 1-4Xyl covalently bound to a Ser residue at the glycosaminylglycan attachment site of proteoglycans.	Uridine Diphosphate Glucuronic Acid	89-98	beta-1,3-glucuronyltransferase 3	Homo sapiens	0-7