Glycosyltransferase engineering for carbohydrate synthesis
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چکیده
منابع مشابه
Engineering a Carbohydrate-processing Transglycosidase into Glycosyltransferase for Natural Product Glycodiversification
Glycodiversification broadens the scope of natural product-derived drug discovery. The acceptor substrate promiscuity of glucosyltransferase-D (GTF-D), a carbohydrate-processing enzyme from Streptococcus mutans, was expanded by protein engineering. Mutants in a site-saturation mutagenesis library were screened on the fluorescent substrate 4-methylumbelliferone to identify derivatives with impro...
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BACKGROUND Oligosaccharide analogues in which the interglycosidic oxygen atom(s) have been replaced by sulfur are known as thiooligosaccharides. These molecules are metabolically stable analogues of their naturally occurring counterparts, since the rate of hydrolysis of the thioglycosidic bond by glycosylhydrolases is several orders of magnitude slower than that of the corresponding Oglycosides...
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The rapid rise of multi-drug-resistant bacteria is a global healthcare crisis, and new antibiotics are urgently required, especially those with modes of action that have low-resistance potential. One promising lead is the liposaccharide antibiotic moenomycin that inhibits bacterial glycosyltransferases, which are essential for peptidoglycan polymerization, while displaying a low rate of resista...
متن کاملOne-step synthesis of novel glycosyltransferase inhibitors.
A one-step synthesis of two 5-CF(3) UDP-sugars is reported. These non-natural sugar-nucleotides are micromolar inhibitors of two different galactosyltransferases.
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Plants produce two flavonoid O-pentoses, flavonoid O-xyloside and flavonoid O-arabinoside. However, analyzing their biological properties is difficult because flavonoids are not naturally produced in sufficient quantities. In this study, Escherichia coli was used to synthesize the plant-specific flavonoid O-pentosides quercetin 3-O-xyloside and quercetin 3-O-arabinoside. Two strategies were use...
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ژورنال
عنوان ژورنال: Biochemical Society Transactions
سال: 2016
ISSN: 0300-5127,1470-8752
DOI: 10.1042/bst20150200