Gu, Jiali published the artcileThe role of aromatic residue W20 in the activity and enantioselectivity control of esterase BioH toward aryl substrate, Product Details of C9H9ClO3, the main research area is Escherichia esterase BioH enantioselectivity aryl substrate methyl chloromandelate; esterase BioH tryptophan phenylalanine aryl substrate pi pi stacking.
Aromatic π-π stacking interaction plays an important role in the enzyme-ligand recognition and stabilization. Esterase BioH, an α/β hydrolase from Escherichia coli, has exhibited potential in the chiral synthesis of alcs. and aryl prochiral diesters. In the present work, the influence of aromatic residue W20 on the activity and enantioselectivity of BioH toward aryl substrates was investigated. Mutation of Trp into Ala or Val led to complete loss of activity, while replacement of Trp by Phe had little effect on the activity and enantioselectivity. Structural and energetic anal. demonstrated that π-π stacking interactions were formed between the residue W20 and the substrate, as well as the residues W20 and F141, which facilitated the stabilization of substrate at the transition state. Moreover, the different probabilities of the parallel-shifted stacking interaction between the residue 20 and R-/S-enantiomer were found related to the enantioselectivity. Thus, it could be concluded that the π-π stacking interaction between the residue W20 and the substrate was crucial in the determination of enzymic catalytic performance. The results not only deepened our understanding in the catalytic mechanism of BioH, but also facilitated further enzyme redesign.
Biochemical Engineering Journal published new progress about Binding energy (BioH – aryl substrate). 32345-60-1 belongs to class chlorides-buliding-blocks, name is (S)-Methyl 2-(2-chlorophenyl)-2-hydroxyacetate, and the molecular formula is C9H9ClO3, Product Details of C9H9ClO3.
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