The structure of the Mycobacterium smegmatis trehalose synthase reveals an unusual active site configuration and acarbose-binding mode(†)

Trehalose synthase (TreS) catalyzes the reversible conversion of maltose into trehalose in mycobacteria as one of three biosynthetic pathways to this nonreducing disaccharide. Given the importance of trehalose to survival of mycobacteria, there has been considerable interest in understanding the enz...

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Hlavní autoři: Caner, Sami, Nguyen, Nham, Aguda, Adeleke, Zhang, Ran, Pan, Yuan T, Withers, Stephen G, Brayer, Gary D
Médium: Artigo
Jazyk:Inglês
Vydáno: Oxford University Press 2013
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Original Articles
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC3724413/
https://ncbi.nlm.nih.gov/pubmed/23735230
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/glycob/cwt044
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