EC Number   |
Protein Variants |
Reference |
|---|
    5.1.2.2 | H297N |
site-directed mutagenesis, analysis of ligand binding, kinetics |
747095 |
| 5.1.2.2 | K166C |
site-directed mutagenesis, analysis of ligand binding, kinetics |
747095 |
| 5.1.2.2 | K166E |
K166R retains low level of racemase activity. K166R mutant catalyzes the elimination of Br- from only the (R)-enantiomer of (R,S)-p-(bromomethyl)mandelate |
285192 |
| 5.1.2.2 | K166M |
site-directed mutagenesis, analysis of ligand binding, kinetics |
747095 |
| 5.1.2.2 | K166M/H297N |
site-directed mutagenesis, analysis of ligand binding, kinetics |
747095 |
| 5.1.2.2 | more |
Comparison of the binding affinities of the mutant variants with the intermediate/transition state analogues benzohydroxamate and cyclohexanecarbohydroxamate reveals that cationPi/N-Pi interactions between His297 and the hydroxamate/hydroximate moiety and the phenyl ring of benzohydroxamate contribute approximately 0.26 and 0.91 kcal/mol to binding, respectively, while interactions with Lys166 contribute approximately 1.74 and 1.74 kcal/mol, respectively. Lys166 contributes over 2.93 kcal/mol to the binding of (R)-atrolactate, and His297 contributes 2.46 kcal/mol to the binding of (S)-atrolactate |
747095 |
| 5.1.2.2 | more |
development and evaluation of a virtual mutant screening method for non-natural substrates based on the binding energy in the transition state, the method is beneficial in enzyme rational redesign and helps to better understand the catalytic properties of the enzyme, and it is effective in predicting the trend of mutational effects on catalysis, molecular dynamic simulation, overview |
727384 |
| 5.1.2.2 | more |
directed evolution of mandelate racemase by a high-throughput screening method, overview |
-, 746856 |
| 5.1.2.2 | more |
evaluation of design of mandelate racemase with higher stability, usage of structural enzyme analysis for reengineering of mandelate racemase for enhanced thermal stability |
742923 |
| 5.1.2.2 | more |
mandelate racemase and mandelate dehydrogenase are coexpressed in Escherichia coli for the synthesis of benzoylformate by converting racemic mandelate |
-, 727197 |
