Directed enzyme evolution and selections for catalysis based on product formation

Journal of Biotechnology
Jean-Luc Jestin, Pierre Alexandre Kaminski

Abstract

Enzyme engineering by molecular modelling and site-directed mutagenesis can be remarkably efficient. Directed enzyme evolution appears as a more general strategy for the isolation of catalysts as it can be applied to most chemical reactions in aqueous solutions. Selections, as opposed to screening, allow the simultaneous analysis of protein properties for sets of up to about 10(14) different proteins. These approaches for the parallel processing of molecular information 'Is the protein a catalyst?' are reviewed here in the case of selections based on the formation of a specific reaction product. Several questions are addressed about in vivo and in vitro selections for catalysis reported in the literature. Can the selection system be extended to other types of enzymes? Does the selection control regio- and stereo-selectivity? Does the selection allow the isolation of enzymes with an efficient turnover? How should substrates be substituted or mimicked for the design of efficient selections while minimising the number of chemical synthesis steps? Engineering sections provide also some clues to design selections or to circumvent selection biases. A special emphasis is put on the comparison of in vivo and in vitro selections for cat...Continue Reading

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Citations

Apr 22, 2010·Molecular Biotechnology·Sophie Vichier-Guerre, Jean-Luc Jestin
Apr 24, 2012·International Journal of Pharmaceutics·Marco G CasteleijnSanjay Sarkhel
Aug 19, 2008·Biochimie·Fariborz Bahrami, Jean-Luc Jestin
May 10, 2008·Biochimie·Jean-Luc Jestin
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Nov 19, 2005·Research in Microbiology·Jean-Luc Jestin, Sophie Vichier-Guerre
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Sep 28, 2005·Organic & Biomolecular Chemistry·Steven J BroadwaterD Tyler McQuade
Oct 12, 2013·Angewandte Chemie·Yunmi LeeEmily P Balskus
Aug 3, 2006·Journal of Agricultural and Food Chemistry·Zhiqiang LiuYong Leng

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