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SLAC Reprint: SLAC-REPRINT-2014-045
SLAC Release Date: April 8, 2014
The Structure of the Mycobacterium smegmatis Trehalose Synthase (TreS) Reveals an Unsual Active Site Configuration and Acarbose Binding Mode
Caner, S.
DOI: 10.1093/glycob/cwt044

Trehalose synthase (TreS) catalyzes the reversible conversion of maltose to trehalose in mycobacteria as one of three biosynthetic pathways to this non-reducing disaccharide. Given the importance of trehalose to survival of mycobacteria there has been con... Show Full Abstract
DOI: 10.1093/glycob/cwt044

Trehalose synthase (TreS) catalyzes the reversible conversion of maltose to trehalose in mycobacteria as one of three biosynthetic pathways to this non-reducing disaccharide. Given the importance of trehalose to survival of mycobacteria there has been considerable interest in understanding the enzymes involved in its production; indeed the structures of the key enzymes in the other two pathways have already been determined. Herein we present the first structure of TreS from Mycobacterium smegmatis, thereby providing insights into the catalytic machinery involved in this intriguing intramolecular reaction. This structure, which is of interest both mechanistically and as a potential pharmaceutical target, reveals a narrow and enclosed active site pocket within which substrate intramolecular rearrangements can occur. We also present the structure of a complex of TreS with acarbose, revealing a hitherto unsuspected oligosaccharide binding site within the C-terminal domain. This may well provide an anchor point for the association of TreS with glycogen, thereby enhancing its role in glycogen biosynthesis and degradation Show Partial Abstract
  • Interest Categories: Bio-life Sciences