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