1.13.11.40	A417G	converts arachidonic acid mainly to 12-hydroxyeicosatetraenoic acid, mutant retains 38% of catalytic efficiency	660365	
1.13.11.40	A417S	same oxygenase specificity and similar catalytic activity to wild-type 8S-LOX	660365	
1.13.11.40	A589M	site-directed mutagenesis, the mutant shows reduced activity and altered protein fold compared to the wild-type enzyme	742865	
1.13.11.40	A592M	stability of the enzyme-substrate complex is similar to wild-type. Contrary to wild-type, hydrogen abstraction from C13 is more favorable in the mutant. A592M yields 19% 8R product, 2% 8S, 60% 11R, 4% 11S, plus some 12R/12S and 15R/15S product	765268	
1.13.11.40	A620H	site-directed mutagenesis, the mutant shows reduced activity and altered protein fold compared to the wild-type enzyme	742865	
1.13.11.40	A623H	stability of the enzyme-substrate complex is similar to wild-type. Contrary to wild-type, hydrogen abstraction from C13 is more favorable in the mutant. A623H yields 16% 8R product, 4% 8S, 57% 11R, 5% 11S, 6% 12R, 6% 12S plus some 15R/15S product	765268	
1.13.11.40	D39A	118% activity compared to the wild type enzyme, mutant with diminished fluorescence resonance energy transfer properties, consistent with a role for calcium in membrane binding	674505	
1.13.11.40	D39A/E47A	106% activity compared to the wild type enzyme, a double mutant with calcium-binding residues from two of the three sites mutated exhibits no fluorescence resonance energy transfer signal	674505	
1.13.11.40	E47A	65% of the activity of the wild type enzyme, mutant with diminished fluorescence resonance energy transfer properties, consistent with a role for calcium in membrane binding	674505	
1.13.11.40	G427A	site-directed mutagenesis. In wild-type, molecular oxygen adds to C8 of arachidonic acid with an R stereochemistry. In the mutant, Ala427 pushes Leu385, blocks the region over C8, and opens an oxygen access channel now directed to C12, where molecular oxygen is added with an S stereochemistry. Thus, the specificity turns out to be dramatically inverted	741487