PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 15078870-2 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 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