Publications by authors named "J O Duus"

Article Synopsis
  • Family 1 glycosyltransferases (GT1s, UGTs) efficiently catalyze the glycosylation of natural products in a single step, with UGT88E3 identified as a strong candidate for creating pure glycosidic products from polyphenols.
  • Research focused on UGT88E3's dual capability of accepting different substrates while maintaining regioselectivity, utilizing techniques like high-field NMR and molecular dynamics simulations.
  • A key finding revealed that a methionine-aromatic bridge in its structure is crucial for its specificity, where mutating the methionine residue at position 127 drastically decreased enzyme activity.
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Daphne mezereum L., an important medicinal plant in Scandinavian folk medicine, was used to treat ailments such as diarrhea, swelling and stomach pain. A range of natural compounds have been isolated, but little attention has been given to the polysaccharides in this plant.

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Engineering glycoside hydrolases is a major route to obtaining catalysts forming glycosidic bonds. Glycosynthases, thioglycoligases, and transglycosylases represent the main strategies, each having advantages and drawbacks. Here, we show that an engineered enzyme from the GH84 family, the acid-base mutant OGA-D120N, is an efficient -, -, and -glycoligase, able to use , , , and nucleophiles.

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Regioselective glycosylation is a chemical challenge, leading to multistep syntheses with protecting group manipulations, ultimately resulting in poor atom economy and compromised sustainability. Enzymes allow eco-friendly and regioselective bond formation with fully deprotected substrates in a single reaction. For the selective glucosylation of silibinin, a pharmaceutical challenged with low solubility, enzyme engineering has previously been employed, but the resulting yields and were limited, prohibiting the application of the engineered catalyst.

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Upon investigation of Streptococcus pneumoniae serotype 15F capsular polysaccharide (CPS), we discovered that it had a different phosphorylation substituent, namely glycerol-2-phosphate like the other serogroup 15 CPS rather than the originally reported 0.2 equivalent of phosphate or phosphocholine. Furthermore, we also determined the locations of the two previously unassigned O-acetyl groups present in the repeating unit of the 15F CPS, and carried out full NMR assignments of the 15F as well as 15A CPS.

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