ArticleACS chemical biology2013
Synthesis of α-glucan in mycobacteria involves a hetero-octameric complex of trehalose synthase TreS and Maltokinase Pep2.
Article in ACS chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 31 citations in OpenAlex.
- A new Persister Enrichment Model inbioRxiv : the preprint server for biology · 2026Article
- Structural and Mutational Analyses of Trehalose Synthase fromJournal of agricultural and food chemistry · 2024Article
- Characterization of Two Glycoside Hydrolases of Family GH13 and GH57, Present in a Polysaccharide Utilization Locus (PUL) ofMolecules (Basel, Switzerland) · 2024Article
- Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes.Chemical reviews · 2024Review
- TargetingACS infectious diseases · 2024Article
- Conservation of the glycogen metabolism pathway underlines a pivotal function of storage polysaccharides in Chlamydiae.Communications biology · 2021Article
- Structure-function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17The Journal of biological chemistry · 2020Article
- Crystal structure of the TreS:Pep2 complex, initiating α-glucan synthesis in the GlgE pathway of mycobacteria.The Journal of biological chemistry · 2019Article
- The N253F mutant structure of trehalose synthase from Deinococcus radiodurans reveals an open active-site topology.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Population Structure and Local Adaptation of MAC Lung Disease Agent Mycobacterium avium subsp. hominissuis.Genome biology and evolution · 2017Article
- Metabolic Network for the Biosynthesis of Intra- and Extracellular α-Glucans Required for Virulence of Mycobacterium tuberculosis.PLoS pathogens · 2016Article
- Structure of mycobacterial maltokinase, the missing link in the essential GlgE-pathway.Scientific reports · 2015Article
- High quality draft genome sequence of Corynebacterium ulceribovis type strain IMMIB-L1395(T) (DSM 45146(T)).Standards in genomic sciences · 2015Article
- Structures of trehalose synthase from Deinococcus radiodurans reveal that a closed conformation is involved in catalysis of the intramolecular isomerization.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Homotypic dimerization of a maltose kinase for molecular scaffolding.Scientific reports · 2014Article
- Article
- The cell envelope glycoconjugates of Mycobacterium tuberculosis.Critical reviews in biochemistry and molecular biologyReview
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8 authors at 2 institutions in 1 country.
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Abstract
Recent evidence established that the cell envelope of Mycobacterium tuberculosis, the bacillus causing tuberculosis (TB), is coated by an α-glucan-containing capsule that has been implicated in persistence in a mouse infection model. As one of three known metabolic routes to α-glucan in mycobacteria, the cytoplasmic GlgE-pathway converts trehalose to α(1 → 4),α(1 → 6)-linked glucan in 4 steps. Whether individual reaction steps, catalyzed by trehalose synthase TreS, maltokinase Pep2, and glycosyltransferases GlgE and GlgB, occur independently or in a coordinated fashion is not known. Here, we report the crystal structure of M. tuberculosis TreS, and show by small-angle X-ray scattering and analytical ultracentrifugation that TreS forms tetramers in solution. Together with Pep2, TreS forms a hetero-octameric complex, and we demonstrate that complex formation markedly accelerates maltokinase activity of Pep2. Thus, complex formation may act as part of a regulatory mechanism of the GlgE pathway, which overall must avoid accumulation of toxic pathway intermediates, such as maltose-1-phosphate, and optimize the use of scarce nutrients.
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