ArticleBiochemistry2014
Structural insight into how Streptomyces coelicolor maltosyl transferase GlgE binds α-maltose 1-phosphate and forms a maltosyl-enzyme intermediate.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 35 citations in OpenAlex.
- Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes.Chemical reviews · 2024Review
- TargetingACS infectious diseases · 2024Article
- Drug Discovery Based on Fluorine-Containing Glycomimetics.Molecules (Basel, Switzerland) · 2023Review
- The Synthesis and Glycoside Formation of Polyfluorinated Carbohydrates.Chemical reviews · 2022Review
- Synthesis of CFrontiers in chemistry · 2022Article
- MonteCarbo: A software to generate and dock multifunctionalized ring molecules.Journal of computational chemistry · 2021Article
- Stereoselective synthesis of a 4-⍺-glucoside of valienamine and its X-ray structure in complex with Streptomyces coelicolor GlgE1-V279S.Scientific reports · 2021Article
- A temperature-sensitive Mycobacterium smegmatis glgE mutation leads to a loss of GlgE enzyme activity and thermostability and the accumulation of α-maltose-1-phosphate.Biochimica et biophysica acta. General subjects · 2021Article
- Structure-function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17The Journal of biological chemistry · 2020Article
- Cell Surface Biosynthesis and Remodeling Pathways in Mycobacteria Reveal New Drug Targets.Frontiers in cellular and infection microbiology · 2020Review
- Zwitterionic pyrrolidene-phosphonates: inhibitors of the glycoside hydrolase-like phosphorylase Streptomyces coelicolor GlgEI-V279S.Organic & biomolecular chemistry · 2017Article
- Ligand-bound Structures and Site-directed Mutagenesis Identify the Acceptor and Secondary Binding Sites of Streptomyces coelicolor Maltosyltransferase GlgE.The Journal of biological chemistry · 2016Article
- Designing sugar mimetics: non-natural pyranosides as innovative chemical tools.Current opinion in chemical biology · 2016Review
- Metabolic Network for the Biosynthesis of Intra- and Extracellular α-Glucans Required for Virulence of Mycobacterium tuberculosis.PLoS pathogens · 2016Article
- Structural Dissection of the Maltodextrin Disproportionation Cycle of the Arabidopsis Plastidial Disproportionating Enzyme 1 (DPE1).The Journal of biological chemistry · 2015Article
- Structure of Mycobacterium thermoresistibile GlgE defines novel conformational states that contribute to the catalytic mechanism.Scientific reports · 2015Article
- Structural Basis for the Interconversion of Maltodextrins by MalQ, the Amylomaltase of Escherichia coli.The Journal of biological chemistry · 2015Article
- Crystal structures of Mycobacterium tuberculosis GlgE and complexes with non-covalent inhibitors.Scientific reports · 2015Article
- Synthesis of 2-deoxy-2,2-difluoro-α-maltosyl fluoride and its X-ray structure in complex with Streptomyces coelicolor GlgEI-V279S.Organic & biomolecular chemistry · 2015Article
- Enzymatic synthesis using glycoside phosphorylases.Carbohydrate research · 2015Review
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Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
Abstract
GlgE (EC 2.4.99.16) is an α-maltose 1-phosphate:(1→4)-α-d-glucan 4-α-d-maltosyltransferase of the CAZy glycoside hydrolase 13_3 family. It is the defining enzyme of a bacterial α-glucan biosynthetic pathway and is a genetically validated anti-tuberculosis target. It catalyzes the α-retaining transfer of maltosyl units from α-maltose 1-phosphate to maltooligosaccharides and is predicted to use a double-displacement mechanism. Evidence of this mechanism was obtained using a combination of site-directed mutagenesis of Streptomyces coelicolor GlgE isoform I, substrate analogues, protein crystallography, and mass spectrometry. The X-ray structures of α-maltose 1-phosphate bound to a D394A mutein and a β-2-deoxy-2-fluoromaltosyl-enzyme intermediate with a E423A mutein were determined. There are few examples of CAZy glycoside hydrolase family 13 members that have had their glycosyl-enzyme intermediate structures determined, and none before now have been obtained with a 2-deoxy-2-fluoro substrate analogue. The covalent modification of Asp394 was confirmed using mass spectrometry. A similar modification of wild-type GlgE proteins from S. coelicolor and Mycobacterium tuberculosis was also observed. Small-angle X-ray scattering of the M. tuberculosis enzyme revealed a homodimeric assembly similar to that of the S. coelicolor enzyme but with slightly differently oriented monomers. The deeper understanding of the structure-function relationships of S. coelicolor GlgE will aid the development of inhibitors of the M. tuberculosis enzyme.
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