Theoretical prediction and experimental verification on enantioselectivity of haloacid dehalogenase l-DEX YL with chloropropionate

- We theoretically analyzed l-2-haloacid dehalogenase from Pseudomonas sp. YL.
- The enzymatic reaction of l-DEX YL to d-2-CPA was compared with that to l-2-CPA.
- QM/MM and FMO calculations suggested Phe60 was an important residue for the catalysis of d-2-CPA.
- The computational results also verified that F60Y mutant's reaction with d-2-CPA could be better.
- The activity assays confirmed that F60Y mutant catalyzed the dehalogenation of d-2-CPA.