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Literature summary for 2.4.1.277 extracted from

  • Borisova, S.A.; Kim, H.J.; Pu, X.; Liu, H.W.
    Glycosylation of acyclic and cyclic aglycone substrates by macrolide glycosyltransferase DesVII/DesVIII: analysis and implications (2008), Chembiochem, 9, 1554-1558.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
medicine the catalytic flexibility of the glycosyltransferase DesVII offers an means for creating new macrolide antibiotics. The substrate flexibility of DesVII/DesVIII is apparently extended to a wide range of linear as well as cyclic substrates. Although the yield of products is notably reduced when unnatural substrates are used, once a desired activity is identified, the catalytic efficiency of these enzymes may be fine-tuned by protein engineering. The substrate flexibility of glycosyltransferases expands the opportunities for glycodiversification to generate new glycoforms of synthetic compounds and macrolide analogues Streptomyces venezuelae

Organism

Organism UniProt Comment Textmining
Streptomyces venezuelae Q9ZGH7
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the macrolide glycosyltransferase, DesVII/DesVIII, can recognize and process not only cyclic substrates of different ring size, but also a variety of linear substrates albeit with reduced, but measurable activities. When multiple hydroxyl groups are present, essentially no regiospecificity is observed for the linear substrates. Only singly glycosylated products are generated in all cases. In contrast, when cyclic substrates with multiple glycosylation sites are tested, the enzyme displays excellent regiospecificity in most cases Streptomyces venezuelae ?
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Synonyms

Synonyms Comment Organism
DesVII/DesVIII
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Streptomyces venezuelae