ArticleMolecular microbiology2013
Enterococcus faecalis utilizes maltose by connecting two incompatible metabolic routes via a novel maltose 6'-phosphate phosphatase (MapP).
Article in Molecular microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 30 citations in OpenAlex.
- Triphala Modulates the Membrane Vesicle Transcriptome of Enterococcus durans VIT3 to Influence Antibiotic Response and Probiotic Functions.Molecular biotechnology · 2026Article
- Cellodextrin Metabolism and Phosphotransferase System-Catalyzed Uptake in Enterococcus faecalis.Molecular microbiology · 2025Article
- Synthesis, radiolabeling, and biological evaluation of methyl 6-deoxy-6-[RSC advances · 2025Article
- The many functions of carbohydrate-active enzymes in family GH65: diversity and application.Applied microbiology and biotechnology · 2024Review
- Inter-species diversity and functional genomic analyses of closed genome assemblies of clinically isolated, megaplasmid-containingAccess microbiology · 2023Article
- In vitro interaction network of a synthetic gut bacterial community.The ISME journal · 2022Article
- Discovery and Biotechnological Exploitation of Glycoside-Phosphorylases.International journal of molecular sciences · 2022Review
- Discovery of a Kojibiose Hydrolase by Analysis of Specificity-Determining Correlated Positions in Glycoside Hydrolase Family 65.Molecules (Basel, Switzerland) · 2021Article
- Enterococcus faecalis Maltodextrin Gene Regulation by Combined Action of Maltose Gene Regulator MalR and Pleiotropic Regulator CcpA.Applied and environmental microbiology · 2020Article
- Cross-utilization of β-galactosides and cellobiose inThe Journal of biological chemistry · 2020Article
- Recovery of the Peptidoglycan Turnover Product Released by the Autolysin Atl inFrontiers in microbiology · 2018Article
- Enzymes Required for Maltodextrin Catabolism in Enterococcus faecalis Exhibit Novel Activities.Applied and environmental microbiology · 2017Article
- Enterococcus faecalis Uses a Phosphotransferase System Permease and a Host Colonization-Related ABC Transporter for Maltodextrin Uptake.Journal of bacteriology · 2017Article
- The bacterial phosphoenolpyruvate:carbohydrate phosphotransferase system: regulation by protein phosphorylation and phosphorylation-dependent protein-protein interactions.Microbiology and molecular biology reviews : MMBR · 2014Review
- Article
- The malQ gene is essential for starch metabolism in Streptococcus mutans.Journal of oral microbiology · 2013Article
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Authors and funding
13 authors at 11 institutions in 5 countries.
Funding
Abstract
Similar to Bacillus subtilis, Enterococcus faecalis transports and phosphorylates maltose via a phosphoenolpyruvate (PEP):maltose phosphotransferase system (PTS). The maltose-specific PTS permease is encoded by the malT gene. However, E. faecalis lacks a malA gene encoding a 6-phospho-α-glucosidase, which in B. subtilis hydrolyses maltose 6'-P into glucose and glucose 6-P. Instead, an operon encoding a maltose phosphorylase (MalP), a phosphoglucomutase and a mutarotase starts upstream from malT. MalP was suggested to split maltose 6-P into glucose 1-P and glucose 6-P. However, purified MalP phosphorolyses maltose but not maltose 6'-P. We discovered that the gene downstream from malT encodes a novel enzyme (MapP) that dephosphorylates maltose 6'-P formed by the PTS. The resulting intracellular maltose is cleaved by MalP into glucose and glucose 1-P. Slow uptake of maltose probably via a maltodextrin ABC transporter allows poor growth for the mapP but not the malP mutant. Synthesis of MapP in a B. subtilis mutant accumulating maltose 6'-P restored growth on maltose. MapP catalyses the dephosphorylation of intracellular maltose 6'-P, and the resulting maltose is converted by the B. subtilis maltose phosphorylase into glucose and glucose 1-P. MapP therefore connects PTS-mediated maltose uptake to maltose phosphorylase-catalysed metabolism. Dephosphorylation assays with a wide variety of phospho-substrates revealed that MapP preferably dephosphorylates disaccharides containing an O-α-glycosyl linkage.
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