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  • Enzymatic glycosylation of vancomycin aglycon: completion of a total synthesis of vancomycin and N- and C-terminus substituent effects of the aglycon substrate.

Enzymatic glycosylation of vancomycin aglycon: completion of a total synthesis of vancomycin and N- and C-terminus substituent effects of the aglycon substrate.

Organic letters (2014-06-24)
Atsushi Nakayama, Akinori Okano, Yiqing Feng, James C Collins, Karen C Collins, Christopher T Walsh, Dale L Boger
ZUSAMMENFASSUNG

Studies on the further development of the sequential glycosylations of the vancomycin aglycon catalyzed by the glycosyltransferases GtfE and GtfD and the observation of unusual, perhaps unexpected, aglycon substrate substituent effects on the rate and efficiency of the initial glycosylation reaction are reported.

MATERIALIEN
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Marke
Produktbeschreibung

Sigma-Aldrich
Vancomycin -hydrochlorid aus Streptomyces orientalis, ≥900 μg per mg (as vancomycin base)
Sigma-Aldrich
Vancomycin -hydrochlorid aus Streptomyces orientalis, ≥85% (Vancomycin B)
Sigma-Aldrich
Vancomycin -hydrochlorid aus Streptomyces orientalis, BioReagent, suitable for plant cell culture
Sigma-Aldrich
Vancomycin -hydrochlorid aus Streptomyces orientalis, meets USP testing specifications
Sigma-Aldrich
Phosphorylase b aus Kaninchenmuskel, lyophilized powder, ≥20 units/mg protein, 2× crystallization
Millipore
Vancomycin-Supplement, suitable for microbiology
Vancomycin -hydrochlorid, European Pharmacopoeia (EP) Reference Standard
Sigma-Aldrich
Phosphorylase b aus Kaninchenmuskel, For use as a marker in SDS-PAGE