EC Number   |
Protein Variants |
Reference |
|---|
   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 | more |
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 | more |
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 |
