A breakthrough in protein engineering of a glycosyltransferase

Reetz, Manfred T.

doi:10.1016/j.gresc.2021.01.007

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A breakthrough in protein engineering of a glycosyltransferase

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Reetz, Manfred T.
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;
Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences;

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Zitation

Reetz, M. T. (2021). A breakthrough in protein engineering of a glycosyltransferase. Green Synthesis and Catalysis, 2(1), 4-5. doi:10.1016/j.gresc.2021.01.007.

Zitierlink: https://hdl.handle.net/21.11116/0000-0008-47C9-6

Zusammenfassung

An intriguing advance in the rational protein engineering of a newly identified glycosyltransferase from Siraitia grosvenorii (UGT74AC2) has been accomplished by Zhoutong Sun, Yuanxia Sun and coworkers for the targeted pharmaceutically significant glucosylation of the polyhydroxy substrate silybin. Using an advanced version of Focused Rational Iterative Site-specific Mutagenesis (FRISM), they were able to evolve mutants that allow the formation of the 3-OH, 7-OH and the 3,7-O-diglycoside products with 94%, > 99% and > 99% regioselectivity, respectively. This can be viewed as a breakthrough because the wildtype UGT74AC2 delivers a difficult to separate mixture of products in a ratio of 22%:39%:39%. Even N- and S-glucosylations were achieved, a likewise unusual accomplishment.