EC Number   |
Protein Variants |
Reference |
|---|
   3.8.1.7 | A112S |
site-directed mutagenesis, overexpression as insoluble protein |
654718 |
| 3.8.1.7 | A112V |
site-directed mutagenesis, overexpression as soluble protein, reduced activity |
654718 |
| 3.8.1.7 | D130A |
site-directed mutagenesis, inactive mutant |
-, 719717 |
| 3.8.1.7 | D145A |
mutant enzymes D145A and H90Q show no catalytic activity, but no effect on ligand binding or the induction of the red shift in the benzoyl ring absorption |
33080 |
| 3.8.1.7 | D184A |
site-directed mutagenesis, inactive mutant |
-, 719717 |
| 3.8.1.7 | D337A |
site-directed mutagenesis, the Km for the mutant Chd increases to 0.176 mM, 50% transformation activity compared to the wild-type Chd |
-, 719717 |
| 3.8.1.7 | D45A |
site-directed mutagenesis, inactive mutant |
-, 719717 |
| 3.8.1.7 | E232D |
mutant enzyme binds the substrate analogue 4-methylbenzoyl-CoA more tightly than does the wild-type dehalogenase. The kcat for 4-chlorobenzoyl-CoS conversion to product is reduced 10000fold in the mutant. Increased sibstrate binding, decreased ring polarization, and decreased catalytic efficiency indicate that the repositioning of the point charge in the Glu232Arg mutant might affect the orientation of the Arg145 carboxylate with respect to the aromatic ring |
667699 |
| 3.8.1.7 | F64A |
site-directed mutagenesis, decreased kcat and slightly increased Km compared to the wild-type enzyme |
654589 |
| 3.8.1.7 | F64L |
The mutant enzymes F64L, F82L, W89F retain substantial catalytic activity the ability to induce the red shift |
-, 33080 |
