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Pelletier, Joelle N.

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Engineering Conferences International

ACCELERATING DISCOVERY OF SUBSTRATE PROMISCUITY IN BIOCATALYZED OXIDATIONS Joelle N. Pelletier, Department of Chemistry, Université de Montréal, Canada Joelle.pelletier@umontreal.ca   Enzymes collectively display a great breadth of catalytic properties yet are individually confined to one or a few specific catalytic tasks. Despite key advances in enzyme engineering, our capacity to predict the effects of mutations on function remains nebulous. Here we present advances in engineering non-native substrate recognition for biocatalyzed transformation into useful products. We examine cytochrome P450 oxidase from Bacillus megaterium (P450 BM3) in its capacity to functionalize C-H bonds. Cost-effective, high-throughput colorimetric screening at the whole-cell level had previously suggested a correlation between the production of indigo and increased substrate promiscuity, in a small number of P450 BM3 variants. We greatly expand the diversity of indigo-producing P450 BM3 variants and demonstrate a correlation with promiscuous aromatic hydroxylation reactions. We look ahead to the potential for large experimental datasets to train smarter design algorithms for enzyme engineering.      Figure 1 – Introduction of  sequence diversity in cytochrome P450 oxidase from Bacillus megaterium (P450 BM3) 

Accelerating Discovery of Substrate Promiscuity in Biocatalyzed Oxidations

https://dc.engconfintl.org/cgi/viewcontent.cgi?filename=0&article=1027&context=enzyme_xxvii&type=additional

Accelerating Discovery of Substrate Promiscuity in Biocatalyzed Oxidations

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Engineering Conferences International