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An article Stereodivergent Protein Engineering of a Lipase To Access All Possible Stereoisomers of Chiral Esters with Two Stereocenters WOS:000468366900037 published article about CANDIDA-ANTARCTICA LIPASE; DIRECTED EVOLUTION; CATALYSIS CONCEPT; METAL CATALYSIS; ENZYMES; ENANTIOSELECTIVITY; TRANSFORMATIONS; CLASSIFICATION; SEQUENCE; FORMS in [Xu, Jian; Cen, Yixin; Fan, Jiajie; Lin, Xianfu; Wu, Qi] Zhejiang Univ, Dept Chem, Hangzhou 310027, Zhejiang, Peoples R China; [Singh, Warispreet; Huang, Meilan] Queens Univ, Sch Chem & Chem Engn, David Keir Bldg,Stranmillis Rd, Belfast BT9 5AG, Antrim, North Ireland; [Cen, Yixin; Wu, Lian; Zhou, Jiahai] Chinese Acad Sci, Shanghai Inst Organ Chem, State Key Lab Bioorgan & Nat Prod Chem, Shanghai 200032, Peoples R China; [Reetz, Manfred T.] Max Planck Inst Kohlenforsch, Kaiser Wilhelm Pl 1, D-45470 Mulheim, Germany; [Reetz, Manfred T.] Philipps Univ, Dept Chem, Hans Meerwein Str 4, D-35032 Marburg, Germany in 2019, Cited 88. The Name is 2-Phenylbutanoic acid. Through research, I have a further understanding and discovery of 90-27-7. Recommanded Product: 90-27-7

Enzymatic stereodivergent synthesis to access all possible product stereoisomers bearing multiple stereocenters is relatively undeveloped, although enzymes are being increasingly used in both academic and industrial areas. When two stereocenters and thus four stereoisomeric products are involved, obtaining stereodivergent enzyme mutants for individually accessing all four stereoisomers would be ideal. Although significant success has been achieved in directed evolution of enzymes in general, stereodivergent engineering of one enzyme into four highly stereocomplementary variants for obtaining the full complement of stereoisomers bearing multiple stereocenters remains a challenge. Using Candida antarctica lipase B (CALB) as a model, we report the protein engineering of this enzyme into four highly stereocomplementary variants needed for obtaining four stereoisomers in transesterification reactions between racemic acids and racemic alcohols in organic solvents. By generating and screening less than 25 variants of each isomer, we achieved >90% selectivity for all of the four possible stereoisomers in the model reaction. This difficult feat was accomplished by developing a strategy dubbed focused rational iterative site-specific mutagenesis (FRISM) at sites lining the enzyme’s binding pocket. The accumulation of single mutations by iterative site-specific mutagenesis using a restricted set of rationally chosen amino acids allows the formation of ultrasmall mutant libraries requiring minimal screening for stereoselectivity. The crystal structure of all stereodivergent CALB variants, flanked by MD simulations, uncovered the source of selectivity.

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