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Updated: Jul 5, 2026

Rapid One-step Enzymatic Synthesis and All-aqueous Purification of Trehalose Analogues
Published on: February 17, 2017
Trehalose synthase converts glycogen to trehalose.
Yuan-Tseng Pan1, J D Carroll, Naoki Asano
1Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, AR 72205, USA.
Trehalose synthase (TreS) in mycobacteria exhibits both amylase and maltose-trehalose interconverting activities, suggesting a novel pathway for trehalose production from glycogen. This enzyme also plays a role in glycogen accumulation.
Area of Science:
- Biochemistry
- Microbiology
- Enzymology
Background:
- Trehalose is crucial for mycobacterial growth.
- Mycobacteria possess multiple trehalose biosynthesis pathways.
- Trehalose synthase (TreS) interconverts trehalose and maltose.
Purpose of the Study:
- To investigate the enzymatic activities of Mycobacterium smegmatis trehalose synthase (TreS).
- To elucidate the role of TreS in trehalose and glycogen metabolism in mycobacteria.
Main Methods:
- Enzyme purification from Mycobacterium smegmatis and recombinant expression in Escherichia coli.
- Assays for maltose-trehalose interconverting (MTase) and amylase activities.
- Enzyme chromatography and crystallization.
- Glycogen accumulation studies in wild-type and mutant mycobacteria.
Main Results:
- TreS exhibits both MTase and amylase activities.
- Amylase activity is stimulated by Ca2+, while MTase is inhibited.
- Validoxylamine inhibits MTase activity, and acarbose inhibits amylase activity.
- TreS facilitates trehalose production from glycogen via maltose.
- TreS is involved in glycogen accumulation in response to high trehalose concentrations.
Conclusions:
- TreS represents a novel pathway for trehalose synthesis from glycogen.
- TreS and trehalose metabolism are interconnected with glycogen production.
- Understanding TreS function offers insights into mycobacterial energy metabolism and survival.
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