3.3.2.6 leukotriene A4 + H2O = leukotriene B4 Asp375 acts as a critical determinant for the stereoselective introduction of the 12R-hydroxyl group, possibly assisted by Gln134 and thus the biological activity of leukotriene B4 647012 3.3.2.6 leukotriene A4 + H2O = leukotriene B4 bifunctional enzyme acting as an epoxide hydrolase and also as an aminopeptidase 646981, 646985, 646986, 646991, 646992, 646993, 646999, 647000, 647001, 647002, 647007, 647009, 647010, 647011, 647012, 647015, 647018, 647019, 647021, 647022 3.3.2.6 leukotriene A4 + H2O = leukotriene B4 enzyme contains two partly overlapping active sites which influence each other 647018, 647021, 647022 3.3.2.6 leukotriene A4 + H2O = leukotriene B4 His295, His299, Glu318, Glu271 are amino acids involved in metallic binding and epoxid hydrolase activity, additional Glu296 and Tyr383 are required for the aminopeptidase activity 647015 3.3.2.6 leukotriene A4 + H2O = leukotriene B4 mechanism 646999 3.3.2.6 leukotriene A4 + H2O = leukotriene B4 mechanistic models, Glu271 is specifically required for the epoxid hydrolase activity and peptidase activity 647011, 647015 3.3.2.6 leukotriene A4 + H2O = leukotriene B4 pathway 647018 3.3.2.6 leukotriene A4 + H2O = leukotriene B4 Ser415 plays a key role in regulating epoxid hydrolase activity 647021 3.3.2.6 leukotriene A4 + H2O = leukotriene B4 the aminopeptidase activity is dependent upon an unmodified cysteine residue, by modifying this cysteine with a small CH3S group it is possible to separate the two enzymatic activities, the aminopeptidase activity and epoxid hydrolase activity, from each other 647022