ArticleThe Journal of biological chemistry2014
Catalytic mechanism and mode of action of the periplasmic alginate epimerase AlgG.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 48 citations in OpenAlex.
- Advances in alginate biosynthesis: regulation and production inFrontiers in bioengineering and biotechnology · 2025Review
- The three-sided right-handed β-helix is a versatile fold for glycan interactions.Glycobiology · 2024Review
- Characterization and Mechanism Study of a Novel PL7 Family Exolytic Alginate Lyase from Marine Bacteria Vibrio sp. W13.Applied biochemistry and biotechnology · 2024Article
- Pseudomonas aeruginosa biofilm exopolysaccharides: assembly, function, and degradation.FEMS microbiology reviews · 2023Review
- Strategy to combat biofilms: a focus on biofilm dispersal enzymes.NPJ biofilms and microbiomes · 2023Review
- Computational modeling of the molecular basis for the calcium-dependence of the mannuronan C-5 epimerase AvAlgE6 fromComputational and structural biotechnology journal · 2023Article
- Structure of the AlgKX modification and secretion complex required for alginate production and biofilm attachment in Pseudomonas aeruginosa.Nature communications · 2022Article
- Mechanistic Basis for Understanding the Dual Activities of the Bifunctional Azotobacter vinelandii Mannuronan C-5-Epimerase and Alginate Lyase AlgE7.Applied and environmental microbiology · 2022Article
- De novo missense variants in FBXO11 alter its protein expression and subcellular localization.Human molecular genetics · 2022Article
- Sequence diversity of theAccess microbiology · 2021Article
- Structural and functional aspects of mannuronic acid-specific PL6 alginate lyase from the human gut microbeThe Journal of biological chemistry · 2019Article
- Immobilization of planktonic algal spores by inkjet printing.Scientific reports · 2019Article
- A new era for understanding amyloid structures and disease.Nature reviews. Molecular cell biology · 2018Review
- De Novo Variants in the F-Box Protein FBXO11 in 20 Individuals with a Variable Neurodevelopmental Disorder.American journal of human genetics · 2018Article
- Biological function of a polysaccharide degrading enzyme in the periplasm.Scientific reports · 2016Article
- Article
- Alginate-modifying enzymes: biological roles and biotechnological uses.Frontiers in microbiology · 2015Review
- Enzymatic modifications of exopolysaccharides enhance bacterial persistence.Frontiers in microbiology · 2015Review
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Authors and funding
7 authors at 5 institutions in 3 countries.
Funding
Abstract
Pseudomonas aeruginosa is an opportunistic pathogen that forms chronic biofilm infections in the lungs of cystic fibrosis patients. A major component of the biofilm during these infections is the exopolysaccharide alginate, which is synthesized at the inner membrane as a homopolymer of 1-4-linked β-D-mannuronate. As the polymer passages through the periplasm, 22-44% of the mannuronate residues are converted to α-L-guluronate by the C5-epimerase AlgG to produce a polymer of alternating β-D-mannuronate and α-L-guluronate blocks and stretches of polymannuronate. To understand the molecular basis of alginate epimerization, the structure of Pseudomonas syringae AlgG has been determined at 2.1-Å resolution, and the protein was functionally characterized. The structure reveals that AlgG is a long right-handed parallel β-helix with an elaborate lid structure. Functional analysis of AlgG mutants suggests that His(319) acts as the catalytic base and that Arg(345) neutralizes the acidic group during the epimerase reaction. Water is the likely catalytic acid. Electrostatic surface potential and residue conservation analyses in conjunction with activity and substrate docking studies suggest that a conserved electropositive groove facilitates polymannuronate binding and contains at least nine substrate binding subsites. These subsites likely align the polymer in the correct register for catalysis to occur. The presence of multiple subsites, the electropositive groove, and the non-random distribution of guluronate in the alginate polymer suggest that AlgG is a processive enzyme. Moreover, comparison of AlgG and the extracellular alginate epimerase AlgE4 of Azotobacter vinelandii provides a structural rationale for the differences in their Ca(2+) dependence.
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