Directed enzyme evolution and selections for catalysis based on product formation.

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 catalysis.

journal_name

J Biotechnol

journal_title

Journal of biotechnology

authors

Jestin JL,Kaminski PA

doi

10.1016/j.jbiotec.2004.03.032

subject

Has Abstract

pub_date

2004-09-30 00:00:00

pages

85-103

issue

1-3

eissn

0168-1656

issn

1873-4863

pii

S0168-1656(04)00308-6

journal_volume

113

pub_type

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