EC Number   |
Protein Variants |
Reference |
|---|
   1.14.14.80 | F434S |
allelic variant, 36% decrease in vamx |
744772 |
| 1.14.14.80 | G130S |
allelic variant, almost inactive |
744772 |
| 1.14.14.80 | K276T |
allelic variant |
744772 |
| 1.14.14.80 | K276T |
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme |
744773 |
| 1.14.14.80 | L509S |
allelic variant, 2.2fold increase in Km |
744772 |
| 1.14.14.80 | more |
construction of two complementary chimera between isoforms CYP4A2-CYP4A3 fused at residue 119 (CYP4A2) and 122 (CYP4A3). The chimera in which the first 119 amino acids are from CYP4A2 indicates that the first 120 amino acids control the substrate specificity. The chimera in which the first 122 amino acids are from CYP4A3 is inactive due to a defect in electron transfer to the heme group |
285382 |
| 1.14.14.80 | P428L |
allelic variant, almost inactive |
744772 |
| 1.14.14.80 | S353G |
allelic variant |
744772 |
| 1.14.14.80 | S353G |
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme |
744773 |
| 1.14.14.80 | V185F |
allelic variant, 4fold increase in Km, 88% decrease in vamx |
744772 |
