EC Number   |
Protein Variants |
Reference  |
|---|
   4.1.99.5 | I24Y |
site-directed mutagenesis, the mutant shows increased activity with n-heptanal compared to the wild-type enzyme |
-, 747351 |
| 4.1.99.5 | I27F |
site-directed mutagenesis, the mutant shows increased activity with n-decanal and n-dodecanal compared to the wild-type enzyme |
747351 |
| 4.1.99.5 | L198F |
site-directed mutagenesis, the mutant shows increased activity with C7-10 aldehydescompared to the wild-type enzyme |
-, 747351 |
| 4.1.99.5 | M193Y |
site-directed mutagenesis, the mutant shows increased activity with C6-10 aldehydes compared to the wild-type enzyme |
747351 |
| 4.1.99.5 | more |
structure-guided protein engineering to alter substrate specificity of aldehyde-deformylating oxygenase towards aldehydes carbon chain length. The impact of the engineered cADO mutants on the change of the hydrocarbon profile is demonstrated by co-expressing acyl-ACP thioesterase BTE, fadD and V184F in Escherichia coli, showing that n-undecane is the main fatty alkane |
-, 747351 |
| 4.1.99.5 | V184F |
site-directed mutagenesis, the mutant shows increased activity with n-dodecanal and n-decanal compared to the wild-type enzyme |
747351 |
| 4.1.99.5 | V28F |
site-directed mutagenesis, the mutant shows increased activity with n-dodecanal compared to the wild-type enzyme |
747351 |
| 4.1.99.5 | Y21R |
site-directed mutagenesis |
-, 747351 |
| 4.1.99.5 | I127G |
site-directed mutagenesis, increased activity compared to wild-type |
-, 747353 |
| 4.1.99.5 | I127G/A48G |
site-directed mutagenesis, increased activity compared to wild-type |
-, 747353 |
