Mutations in the stereospecificity pocket and at the entrance of the active site of Candida antarctica lipase B enhancing enzyme enantioselectivity

…, C Bauer, S Lamare, K Hult, V Tranc, M Graber

Index: Marton; Leonard-Nevers; Syren; Bauer; Lamare; Hult; Tranc; Graber Journal of Molecular Catalysis B: Enzymatic, 2010 , vol. 65, # 1-4 p. 11 - 17

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Citation Number: 26

Abstract

Two different parts of Candida antarctica lipase B (stereospecificity pocket at the bottom of the active site and hydrophobic tunnel leading to the active site) were redesigned by single- or double-point mutations, in order to better control and improve enzyme enantioselectivity toward secondary alcohols. Single-point isosteric mutations of Ser47 and Thr42 situated in the stereospecificity pocket gave rise to variants with doubled enantioselectivity toward ...