Enzymes in organic synthesis: use of subtilisin and a highly stable mutant derived from multiple site-specific mutations

CH Wong, ST Chen, WJ Hennen, JA Bibbs…

Index: Wong; Chen; Hennen; Bibbs; Wang; L iu; Pantoliano; Whitlow; Bryan Journal of the American Chemical Society, 1990 , vol. 112, # 3 p. 945 - 953

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Citation Number: 173

Abstract

Abstract: A subtilisin mutant (subtilisin 8350) derived from subtilisin BPN'via six site-specific mutations (MetSOPhe, Gly169Ala, Asn76Asp, Gln206Cys, Tyr217Lys, and Asn218Ser) was found to be 100 times more stable than the wild-type enzyme in aqueous solution at room temperature and 50 times more stable than the wild type in anhydrous dimethylformamide. Kinetic studies using ester, thio ester, and amide substrates, and the transition-state ...

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