3.3.2.6	Br-	stimulates peptidase and epoxide hydrolase activity (i.e. conversion of leukotriene A4 into leukotriene B4), SCN- most effective, followed by Cl- and Br-	646992	
3.3.2.6	Cl-	stimulates peptidase activity, not epoxide hydrolase activity (i.e. conversion of leukotriene A4 into leukotriene B4), SCN- most effective, followed by Cl- and Br-	646992	
3.3.2.6	Co2+	apoenzyme can be restored by addition of Co2+, peptidase activity exceeds that of enzyme reactivated with zinc	646986	
3.3.2.6	Co2+	apoenzyme is inactive and can be reactivated by addition of stoichiometric amounts of zinc and cobalt	646993	
3.3.2.6	thiocyanate	stimulates peptidase and epoxide hydrolase activity (i.e. conversion of leukotriene A4 into leukotriene B4), SCN- most effective, followed by Cl- and Br-	646992	
3.3.2.6	Zinc	-	647009	
3.3.2.6	Zinc	0.8 mol zinc per mol enzyme	647009	
3.3.2.6	Zinc	apoenzyme is inactive and can be reactivated by addition of stoichiometric amounts of zinc and cobalt	646993	
3.3.2.6	Zinc	catalytic zinc site with the signature HEXXH-(X)18-E, three zinc binding ligands: His295, His299 and Glu318	647015	
3.3.2.6	Zinc	recombinant enzyme: 0.7-1 mol of zinc/mol of enzyme	646985	
3.3.2.6	Zinc	small intestine: 0.99 mol of zinc/mol of enzyme	646985	
3.3.2.6	Zinc	the sequence that codes for the zinc-ion-binding motif is identical in the short-from and long-form enzyme mRNAs	647016	
3.3.2.6	Zinc	three putative zinc-binding ligands: His340, His344 and Glu363, zinc atom is catalytic and also involved in the maintenance of the structural integrity of the enzyme	647010	
3.3.2.6	Zinc	zinc content: 1 mol of zinc per mol of enzyme	646984, 646993, 647015	
3.3.2.6	Zinc	zinc protein	646984, 646985, 646986, 646993, 646995, 646996, 646999, 647000, 647001, 647002, 647003, 647005, 647006, 647007, 647008, 647010, 647014, 647015, 647016, 647017, 647019, 647022	
3.3.2.6	Zn2+	-	683960, 684016	
3.3.2.6	Zn2+	contains zinc	698790, 699434, 731439, 731445, 731641, 731746	
3.3.2.6	Zn2+	contains Zn2+	732701	
3.3.2.6	Zn2+	contans zinc	731116	
3.3.2.6	Zn2+	leukotriene A4 hydrolase is a zinc metalloenzyme	753500	
3.3.2.6	Zn2+	LTA4-h is a bifunctional zinc-dependent metalloenzyme	696718	
3.3.2.6	Zn2+	LTA4H is a zinc metalloprotease	707687	
3.3.2.6	Zn2+	the enzyme contains zinc	697288	
3.3.2.6	Zn2+	the zinc ion is essential for both catalytic activities of LTA4H, it is coordinated by three amino acid residues (His295, His299, Glu318) located in the catalytic domain	752956	
3.3.2.6	Zn2+	zinc metalloenzyme	731360, 732830	
3.3.2.6	Zn2+	zinc metalloenzyme, enzyme LTA4H folds into three domains and creates a deep cleft harboring the catalytic Zn2+ site, forming the active site with an L-shaped hydrophobic pocket deep into the protein	754386