PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15078870-2	2004	In the x-ray crystal structure of LTA(4) hydrolase, Arg(563) and Lys(565) are found at the entrance of the active center.	Arginine	52-55	leukotriene A4 hydrolase	Homo sapiens	34-50	
24573245-3	2014	We have found that the best proteinogenic amino acid recognized by LTA4H is arginine.	Arginine	76-84	leukotriene A4 hydrolase	Homo sapiens	67-72	
16024909-3	2005	Here we used a modeled structure of S. cerevisiae LTA4 hydrolase, mutational analysis, and binding studies to show that Glu-316 and Arg-627 are critical for catalysis, allowing us to a propose a mechanism for the epoxide hydrolase activity.	Arginine	132-135	leukotriene A4 hydrolase	Homo sapiens	50-64	
15078870-10	2004	In conclusion, Arg(563) and Lys(565) possess distinct roles as carboxylate recognition sites for two chemically different substrates, each of which is turned over in separate enzymatic reactions catalyzed by LTA(4) hydrolase.	Arginine	15-18	leukotriene A4 hydrolase	Homo sapiens	208-224