September 24-28, 2017
Aminotransferases are widely exploited in simple as well as more elaborate multi-enzymatic cascade reactions as an environmentally friendly alternative to transition metal catalysis. However, efficient selective conversion of numerous targets is a great limitation to date . Attempts to improve substrate scope have been undertaken by generation and screening of large mutant libraries, which is very time-consuming and raises costs concerns . Recent approaches explored the use of molecular docking of demanding substrates, followed by energy minimization and/or MD simulations [1;3]. Still, the best results have been obtained by extensive mutagenesis and screening.
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Elisa Lanfranchi, Hein J. Wijma, Dick B. Janssen, Carlos J. Ramírez, and Madhurya Lutikurti, "Computational redesign of transaminase active site" in "Enzyme Engineering XXIV", Pierre Monsan, Toulouse White Biotechnology, France Magali Remaud-Simeon, LISBP-INSA, University of Toulouse, France Eds, ECI Symposium Series, (2017). http://dc.engconfintl.org/enzyme_xxiv/38