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• W2807574667 abstract "A structure-guided engineering of fructose-6-phosphate aldolase was performed to expand its substrate promiscuity toward aliphatic nucleophiles, that is, unsubstituted alkanones and alkanals. A smart combinatorial library was created targeting residues D6, T26, and N28, which form a binding pocket around the nucleophilic carbon atom. Double-selectivity screening was executed by high-performance TLC that allowed simultaneous determination of total activity as well as a preference for acetone versus propanal as competing nucleophiles. D6 turned out to be the key residue that enabled activity with non-hydroxylated nucleophiles. Altogether 25 single- and double-site variants (D6X and D6X/T26X) were discovered that show useful synthetic activity and a varying preference for ketone or aldehyde as the aldol nucleophiles. Remarkably, all of the novel variants had completely lost their native activity for cleavage of fructose 6-phosphate." @default.
• W2807574667 created "2018-06-13" @default.
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• W2807574667 date "2018-07-04" @default.
• W2807574667 modified "2023-10-14" @default.
• W2807574667 title "Complete Switch of Reaction Specificity of an Aldolase by Directed Evolution In Vitro: Synthesis of Generic Aliphatic Aldol Products" @default.
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• W2807574667 doi "https://doi.org/10.1002/anie.201804831" @default.
• W2807574667 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6099348" @default.
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