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- W2804103075 abstract "To improve the specific activity and catalytic efficiency of l-LcLDH1, an NADH-dependent allosteric l-lactate dehydrogenase from L. casei, towards phenylpyruvic acid (PPA), its directed modification was conducted based on the semi-rational design. The three variant genes, Lcldh1Q88R, Lcldh1I229A and Lcldh1T235G, were constructed by whole-plasmid PCR as designed theoretically, and expressed in E. coli BL21(DE3), respectively. The purified mutant, l-LcLDH1Q88R or l-LcLDH1I229A, displayed the specific activity of 451.5 or 512.4 U/mg towards PPA, by which the asymmetric reduction of PPA afforded l-phenyllactic acid (PLA) with an enantiomeric excess (eep) more than 99%. Their catalytic efficiencies (kcat/Km) without d-fructose-1,6-diphosphate (d-FDP) were 4.8- and 5.2-fold that of l-LcLDH1. Additionally, the kcat/Km values of l-LcLDH1Q88R and l-LcLDH1I229A with d-FDP were 168.4- and 8.5-fold higher than those of the same enzymes without d-FDP, respectively. The analysis of catalytic mechanisms by molecular docking (MD) simulation indicated that substituting I229 in l-LcLDH1 with Ala enlarges the space of substrate-binding pocket, and that the replacement of Q88 with Arg makes the inlet of pocket larger than that of l-LcLDH1." @default.
- W2804103075 created "2018-06-01" @default.
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- W2804103075 date "2018-09-01" @default.
- W2804103075 modified "2023-09-26" @default.
- W2804103075 title "Directed modification of l - Lc LDH1, an l -lactate dehydrogenase from Lactobacillus casei , to improve its specific activity and catalytic efficiency towards phenylpyruvic acid" @default.
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- W2804103075 doi "https://doi.org/10.1016/j.jbiotec.2018.05.011" @default.
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