61597-99-7Relevant articles and documents
Single-Point Mutant Inverts the Stereoselectivity of a Carbonyl Reductase toward β-Ketoesters with Enhanced Activity
Li, Aipeng,Wang, Ting,Tian, Qing,Yang, Xiaohong,Yin, Dongming,Qin, Yong,Zhang, Lianbing
, p. 6283 - 6294 (2021/03/16)
Enzyme stereoselectivity control is still a major challenge. To gain insight into the molecular basis of enzyme stereo-recognition and expand the source of antiPrelog carbonyl reductase toward β-ketoesters, rational enzyme design aiming at stereoselectivity inversion was performed. The designed variant Q139G switched the enzyme stereoselectivity toward β-ketoesters from Prelog to antiPrelog, providing corresponding alcohols in high enantiomeric purity (89.1–99.1 % ee). More importantly, the well-known trade-off between stereoselectivity and activity was not found. Q139G exhibited higher catalytic activity than the wildtype enzyme, the enhancement of the catalytic efficiency (kcat/Km) varied from 1.1- to 27.1-fold. Interestingly, the mutant Q139G did not lead to reversed stereoselectivity toward aromatic ketones. Analysis of enzyme–substrate complexes showed that the structural flexibility of β-ketoesters and a newly formed cave together facilitated the formation of the antiPrelog-preferred conformation. In contrast, the relatively large and rigid structure of the aromatic ketones prevents them from forming the antiPrelog-preferred conformation.
Biochemical reduction of 3-oxoalkanoic esters by a bottom-fermentation yeast, Saccharomyces cerevisiae IFO 0565
Mochizuki,Sugai,Ohta
, p. 1666 - 1670 (2007/10/02)
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ENHANCED OPTICAL PURITY OF 3-HYDROXYESTERS OBTAINED BY BAKER'S YEAST REDUCTION OF 3-KETOESTERS
Spiliotis, Vassilis,Papahatjis, Demetris,Ragoussis, Nikitas
, p. 1615 - 1616 (2007/10/02)
Fermenting Baker's yeast, enclosed in a dialysis tube, reduces efficiently 3-ketoesters added to the surrounding subtonic solution, to the corresponding 3-hydroxyesters in good yield (45-55percent) and enhanced optical purity (ee 96-97percent)
