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Publication Abstract from PubMed

Trehalose synthase (TreS) catalyzes the reversible interconversion of maltose to trehalose, playing a vital role in trehalose production. Understanding the catalytic mechanism of TreS is crucial for optimizing the enzyme activity and enhancing its suitability for industrial applications. Here, we report the crystal structures of both the wild type and the E324D mutant of Deinococcus radiodurans trehalose synthase in complex with the trehalose analogue, validoxylamine A. By employing structure-guided mutagenesis, we identified N253, E320, and E324 as crucial residues within the +1 subsite for isomerase activity. Based on these complex structures, we propose the catalytic mechanism underlying the reversible interconversion of maltose to trehalose. These findings significantly advance our comprehension of the reaction mechanism of TreS.

Structural and Mutational Analyses of Trehalose Synthase from Deinococcus radiodurans Reveal the Interconversion of Maltose-Trehalose Mechanism.,Ye LC, Chow SY, Chang SC, Kuo CH, Wang YL, Wei YJ, Lee GC, Liaw SH, Chen WM, Chen SC J Agric Food Chem. 2024 Aug 21;72(33):18649-18657. doi: 10.1021/acs.jafc.4c03661. , Epub 2024 Aug 7. PMID:39109746^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.