1.13.11.B6	A562G	site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme	724736	
1.13.11.B6	A562G	the mutation does not affect the relative yield of 13-hydroperoxide, but increases the proportion of (13R)-enantiomer compared to the wild-type enzyme	724736	
1.13.11.B6	F580A	kcat/KM for linoleate hydroperoxidation is increased by 35%	703535	
1.13.11.B6	F580A	possesses activity profile that is similar to wild-type	703535	
1.13.11.B6	F580V	possesses activity profile that is similar to wild-type	703535	
1.13.11.B6	G567A	site-directed mutagenesis, the mutant converts the dual positional specific LOX1:Md:1a to an enzyme with a high specificity for 9(S)-hydroperoxide formation	742627	
1.13.11.B6	G567A	site-directed mutagenesis, the mutant converts the dual positional specific LOX1:Md:1a to an enzyme with a high specificity for 9(S)-hydroperoxide formation, mutant substrate specificity compared to the wild-type enzyme, chiral analysis	742627	
1.13.11.B6	I437L	KM-value for linoleate is 114% of wild-type value, kcat/Km for linoleate is 83% of wild-type value. Positional specificity 13-hydroperoxy-(10E,12Z)-octadecadienoate/9-hydroperoxy-(10E,12Z)-octadecadienoate is 0.7 (compared to 0.8 in reaction with wild-type enzyme)	396190	
1.13.11.B6	I566F	site-directed mutagenesis, inactive mutant	742627	
1.13.11.B6	I578L	site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme, chiral analysis	742627