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Dr. Madhura Rale, Dr. Sarah Schneider, Prof. Dr. Georg A. Sprenger, Dr. Anne K. Samland and Prof. Dr. Wolf-Dieter Fessner Broadening Deoxysugar Glycodiversity: Natural and Engineered Transaldolases Unlock a Complementary Substrate Space Chemistry - A European Journal 17

Version of Record online: 2 FEB 2011 | DOI: 10.1002/chem.201002942

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Increased glycodiversity: Together, the engineered transaldolase TalBF178Y and wild-type FSA from E. coli offer an exceptionally broad and completely stereoselective access to variously deoxygenated sugar-type products (see figure). The enzymes complement each other's aldol donor substrate selectivity, which has allowed the preparation, out of a [3×8] substrate matrix, of a 22-membered library of ketoses, many of which are inaccessible by available enzymes.

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