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	
1.13.11.B6	K578/T579RS	possesses activity profile that is similar to wild-type	703535	
1.13.11.B6	L350M	site-directed mutagenesis, the mutant shows increased specificity for 13S-lipoxygenation, EC 1.13.11.12, altered substrate specificity/regiospecific activity, overview	-, 725658	
1.13.11.B6	L569V	kcat/KM for linoleate hydroperoxidation is reduced by 38%	703535	
1.13.11.B6	L572I	site-directed mutagenesis, inactive mutant	742627	
1.13.11.B6	additional information	mutants Arg268Ala, Gly567Ala, Ile578Leu and Val582Phe show high substrate conversion rates of linoleate, linolenate and arachidonate (60%-100% of wild-type LOX1:Md:1a activity with linoleate). Substrate specificity of mutants, overview	742627	
1.13.11.B6	additional information	replacement Leu350 in 9S-MnLOX and changes the regiospecific oxidation of 18:2 n-6 in a consistent way, but the n-3 double bond of 18:3 n-3 can reduce this effect	-, 725658	
1.13.11.B6	Q599F	the wild-type enzyme is a linoleate 13-LOX above pH 7.5, below this value it functions as a linoleate 9-LOX. The mutant loses its 13-LOX activity at higher pH-values. At pH-values above 7.5 a rather unspecific product pattern (1:1 ratio of 13-hydroperoxy-(10E,12Z)-octadecadienoate and 9-hydroperoxy-(10E,12Z)-octadecadienoate) is observed with the mutant enzyme. The unspecific oxygenation reaction is also indicated by the R/S-ratio (4:6) of the major reaction products	706122	
1.13.11.B6	Q599H	the mutation converts the enzyme to a linoleate 13-LOX lacking any pH sensitivity. The pH optimum remains unaffected, and the major product isomers are in the S-configuration	706122	
1.13.11.B6	R268A	site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme, chiral analysis	742627	
1.13.11.B6	T579F	kcat/KM for linoleate hydroperoxidation is reduced by 89%	703535	
1.13.11.B6	T579S	possesses activity profile that is similar to wild-type	703535	
1.13.11.B6	V570I	KM-value for linoleate is 61% of wild-type value, kcat/Km for linoleate is 367% of wild-type value. Positional specificity 13-hydroperoxy-(10E,12Z)-octadecadienoate/9-hydroperoxy-(10E,12Z)-octadecadienoate is 0.6 (compared to 0.8 in reaction with wild-type enzyme)	396190	
1.13.11.B6	V570I	possesses activity profile that is similar to wild-type	703535	
1.13.11.B6	V580F	KM-value for linoleate is 384% of wild-type value, kcat/Km for linoleate is 4% of wild-type value. Positional specificity 13-hydroperoxy-(10E,12Z)-octadecadienoate/9-hydroperoxy-(10E,12Z)-octadecadienoate is 0.9 (compared to 0.8 in reaction with wild-type enzyme)	396190	
1.13.11.B6	V582F	site-directed mutagenesis, mutant substrate specificity compared to the wild-type enzyme, chiral analysis	742627	
1.13.11.B6	W523A	kcat/KM for linoleate hydroperoxidation is reduced by 98%	703535