EC Number   |
Protein Variants |
Reference  |
|---|
   4.1.3.43 | H20A |
mutant generated by site-directed mutagenesis, pH profiles show the dependence of enzyme activity on hydroxide concentration |
714244 |
| 4.1.3.43 | H20S |
mutant generated by site-directed mutagenesis, pH profiles show the dependence of enzyme activity on hydroxide concentration |
714244 |
| 4.1.3.43 | L87A |
mutant generated by site-directed mutagenesis, variant exhibits a 40fold preference for propionaldehyde over acetaldehyde in contrast to wild type with similar specificities for acetaldehyde and propionaldehyde |
714244 |
| 4.1.3.43 | L89A |
mutant generated by site-directed mutagenesis, specificity constant of this variant in the aldol addition reaction using pentaldehyde is increased approx. 50fold, making it more catalytically efficient for pentaldehyde utilization compared to the wild-type utilization of the natural substrate, acetaldehyde |
714244 |
| 4.1.3.43 | R16A |
mutant generated by site-directed mutagenesis, no detectable aldol cleavage and pyruvate R-proton exchange, supporting the role of Arg-16 in stabilizing a pyruvate enolate intermediate |
714244 |
| 4.1.3.43 | Y290F |
mutant generated by site-directed mutagenesis, mutation results in a loss of stereochemical control as the variant is able to utilize substrates with R and S configurations at C4 with similar kinetic parameters |
714244 |
| 4.1.3.43 | Y290S |
mutant generated by site-directed mutagenesis, mutation results in a loss of stereochemical control as the variant is able to utilize substrates with R and S configurations at C4 with similar kinetic parameters |
714244 |
| 4.1.3.43 | G322A |
channels acetaldehyde with similar efficiency to wild-type, 30% lowered efficiency of isobutyraldehyde channeling |
721651 |
| 4.1.3.43 | G322F |
unable to channel either acetaldehyde or propionaldehyde |
721651 |
| 4.1.3.43 | G322L |
unable to channel either acetaldehyde or propionaldehyde |
721651 |
