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• W3120517849 abstract "To enhance the specific activity and catalytic efficiency (kcat/Km) of an NADH-dependent LpPPR, its directed modification was performed based on the computer-aided design using molecular docking simulation and multiple sequence alignment. Firstly, five single-site variants of an LpPPR-encoding gene (lpppr) were amplified and expressed in E. coli BL21 (DE3). The asymmetric reduction of 20 mM phenylpyruvic acid (PPA) was carried out using 50 mg/mL E. coli/lppprR53Q or /lppprA79V whole wet cells at 37 °C for 20 min, giving d-phenyllactic acid (PLA) with 41.1 or 44.3% yield, being 1.17- or 1.26-fold that by E. coli/lpppr. Secondly, double-site variants were obtained by saturation mutagenesis of Ala79 in LpPPRR53Q. Among all tested E. coli transformants, E. coli/lppprR53Q/A79V exhibited the highest d-PLA yield of 85.3%. The specific activity and kcat/Km of the purified LpPPRR53Q/A79V increased to 67.5 U/mg and 169.8 mM-1 s-1, which were 3.0- and 13.2-fold those of LpPPR, respectively. Finally, the catalytic mechanism analysis of LpPPRR53Q/A79V by molecular docking simulation indicated that the replacement of Arg53 in LpPPR with Gln expanded its substrate-binding pocket, while that Ala79 with Val formed an additional π-sigma interaction with phenyl group of PPA.The online version of this article (10.1007/s13205-020-02633-3) contains supplementary material, which is available to authorized users." @default.
• W3120517849 created "2021-01-18" @default.
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• W3120517849 date "2021-01-13" @default.
• W3120517849 modified "2023-10-16" @default.
• W3120517849 title "Improvement in the catalytic performance of a phenylpyruvate reductase from Lactobacillus plantarum by site-directed and saturation mutagenesis based on the computer-aided design" @default.
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• W3120517849 doi "https://doi.org/10.1007/s13205-020-02633-3" @default.
• W3120517849 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7806690" @default.
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