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• W4238165763 endingPage "13189" @default.
• W4238165763 startingPage "13184" @default.
• W4238165763 abstract "Chemoenzymatic routes toward complex glycoconjugates often depend on the availability of sugar-1-phosphates. Yet the chemical synthesis of these vital components is often tedious, whereas natural enzymes capable of anomeric phosphorylation are known to be specific for one or only a few monosaccharides. Herein we describe the application of directed evolution and a high-throughput multisugar colorimetric screen to enhance the catalytic capabilities of the Escherichia coli galactokinase GalK. From this approach, one particular GalK mutant carrying a single amino acid exchange (Y371H) displayed a surprisingly substantial degree of kinase activity toward sugars as diverse as d -galacturonic acid, d -talose, l -altrose, and l -glucose, all of which failed as wild-type GalK substrates. Furthermore, this mutant provides enhanced turnover of the small pool of sugars converted by the wild-type enzyme. Comparison of this mutation to the recently solved structure of Lactococcus lactis GalK begins to provide a blueprint for further engineering of this vital class of enzyme. In addition, the rapid access to such promiscuous sugar C-1 kinases will significantly enhance accessibility to natural and unnatural sugar-1-phosphates and thereby impact both in vitro and in vivo glycosylation methodologies, such as natural product glycorandomization." @default.
• W4238165763 created "2022-05-12" @default.
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• W4238165763 date "2003-10-31" @default.
• W4238165763 modified "2023-10-16" @default.
• W4238165763 title "Creation of the first anomeric <scp>d</scp> / <scp>l</scp> -sugar kinase by means of directed evolution" @default.
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• W4238165763 doi "https://doi.org/10.1073/pnas.100.23.13184" @default.
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