PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25236239-1	2015	A mutant derived from a cyclodextrin glucantransferase with an alanine residue as its acid/base catalyst residue (CGT-E284A) catalyzed regioselective glycosylation at 3-OH of l-ascorbic acid using alpha-maltosyl fluoride (alphaG2F) and l-ascorbic acid as the donor and acceptor, respectively, yielding 3-O-alpha-maltosyl-l-ascorbate (AA3alphaG2).	Alanine	63-70	UDP glycosyltransferase 8	Homo sapiens	114-117	
24274477-2	2014	In this paper, we describe another example, wherein a cyclodextrin glucanotransferase mutant (CGT-E284A) with an alanine residue at its general acid/base catalyst position (Glu284), was constructed.	Alanine	113-120	UDP glycosyltransferase 8	Homo sapiens	94-97	
24274477-5	2014	Through a thin-layer chromatography-based screening process, two mutants were identified; (1) a mutant with a glycine residue at Glu284 (CGT-E284G) exhibiting improved transglycosylation activity compared with the original alanine mutant and (2) a mutant with a serine residue with residual hydrolytic activity.	Alanine	223-230	UDP glycosyltransferase 8	Homo sapiens	137-140