PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15485660-2	2004	In vivo only beta-hexosaminidase A can utilize GM2 ganglioside as a substrate, but requires the GM2 activator protein to bind GM2 ganglioside and then interact with the enzyme, placing the terminal GalNAc residue in the active site of the alpha-subunit.	N-acetylgalactosaminuronic acid	198-204	O-GlcNAcase	Homo sapiens	13-32	
11148210-5	2001	The cloned O-GlcNAcase has a pH optimum of 5.5-7.0 and is inhibited by GlcNAc but not by GalNAc.	N-acetylgalactosaminuronic acid	89-95	O-GlcNAcase	Homo sapiens	11-22	
3931626-9	1985	We propose that some, if not all, of the sulphated N-acetylhexosamine present in human urine is derived from the action of beta-N-acetylhexosaminidase on sulphated GlcNAc or GalNAc residues at the non-reducing end of keratan sulphate, dermatan sulphate or chondroitin sulphate.	N-acetylgalactosaminuronic acid	174-180	O-GlcNAcase	Homo sapiens	123-150	
27422836-3	2016	A beta-N-acetylhexosaminidase named BbhI, which belongs to glycoside hydrolase family 20 and was obtained from B. bifidum JCM 1254, possesses the bifunctional property of efficiently transferring both GalNAc and GlcNAc residues through beta1-3 linkage to the Gal residue of lactose.	N-acetylgalactosaminuronic acid	201-207	O-GlcNAcase	Homo sapiens	2-29