PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11917124-3	2002	From the crystal structure of LTA4H, a hydrophilic patch composed of Gln-134, Tyr-267, and Asp-375 was identified in a narrow and otherwise hydrophobic pocket, believed to bind LTA4.	Glutamine	69-72	leukotriene A4 hydrolase	Homo sapiens	30-35	
11675384-3	2002	Recently, the structure of leukotriene A(4) hydrolase revealed that Glu-271, which belongs to a conserved GXMEN motif in the M1 family of zinc peptidases, and Gln-136 are located at the active site.	Glutamine	159-162	leukotriene A4 hydrolase	Homo sapiens	27-53	
1516710-7	1992	The mutant E297Q (Glu changed to Gln) conserved LTA4 hydrolase activity but showed little aminopeptidase activity.	Glutamine	33-36	leukotriene A4 hydrolase	Homo sapiens	48-62	
1516710-9	1992	It is thus proposed that either a glutamic or glutamine moiety at 297 is required for full LTA4 hydrolase activity, while the free carboxylic acid of glutamic acid is essential for aminopeptidase.	Glutamine	46-55	leukotriene A4 hydrolase	Homo sapiens	91-105	
22411732-6	2012	Analogous Glu-Asn pair in tricon interacting factor F3 (F3) and Gln-Asn pair in human leukotriene A(4) hydrolase (LTA(4) H) are also conserved in respective homologs.	Glutamine	64-67	leukotriene A4 hydrolase	Homo sapiens	86-112	
22411732-6	2012	Analogous Glu-Asn pair in tricon interacting factor F3 (F3) and Gln-Asn pair in human leukotriene A(4) hydrolase (LTA(4) H) are also conserved in respective homologs.	Glutamine	64-67	leukotriene A4 hydrolase	Homo sapiens	114-122	
8358013-6	1993	Single amino acid substitutions at Glu-297 revealed a distinction of two enzyme activities, and suggest that the glutamic acid residue at 297 is essential for aminopeptidase, while the side chain of Glu or Gln is required for LTA4 hydrolase activity.	Glutamine	206-209	leukotriene A4 hydrolase	Homo sapiens	226-240