ReviewApplied and environmental microbiology2018
Diversity of Three-Dimensional Structures and Catalytic Mechanisms of Alginate Lyases.
Review in Applied and environmental microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
53 citing papers in PubMed, 100 citations in OpenAlex.
- A specific tripartite tricarboxylate transporter is involved in alginate utilization byApplied and environmental microbiology · 2026Article
- Sodium Alginate Modifications: A Critical Review of Current Strategies and Emerging Applications.Foods (Basel, Switzerland) · 2025Review
- Characterization of Alginate Utilization Strategy in a Novel MarineMarine drugs · 2025Article
- Role of Enzyme Technologies and Applied Enzymology in Valorising Seaweed Bioproducts.Marine drugs · 2025Review
- Characterization of a novel alginate lyase Alg0392 with organic solvent-tolerance from Alteromonas sp. A1-6.Applied microbiology and biotechnology · 2025Article
- Diatom heterotrophy on brown algal polysaccharides emerged through horizontal gene transfer, gene duplication, and neofunctionalization.PLoS biology · 2025Article
- Unraveling the molecular mechanism of polysaccharide lyases for efficient alginate degradation.Nature communications · 2025Article
- Multi-Functional Alginate LyaseMarine drugs · 2025Article
- Potential role of alginate in marine bacteria-yeast interactions.Applied and environmental microbiology · 2024Article
- A comparative study of the efficacy of alginate lyases in the presence of metal ions elevated in the cystic fibrosis lung milieu.Biochemistry and biophysics reports · 2024Article
- Expression, Purification, and Characterisation of Recombinant Alginate Lyase (Molecules (Basel, Switzerland) · 2024Article
- Alginate-Degrading Modes, Oligosaccharide-Yielding Properties, and Potential Applications of a Novel Bacterial Multifunctional Enzyme, Aly16-1.Microorganisms · 2024Article
- A "Pro-Asp-Thr" Amino Acid Repeat fromInternational journal of molecular sciences · 2024Article
- Article
- Metagenomic insights into the dynamic degradation of brown algal polysaccharides by kelp-associated microbiota.Applied and environmental microbiology · 2024Article
- A bifunctional endolytic alginate lyase with two different lyase catalytic domains fromFrontiers in microbiology · 2024Article
- Genome Sequencing-Based Mining and Characterization of a Novel Alginate Lyase fromMarine drugs · 2023Article
- Effects of Different Nitrogen Levels on Lignocellulolytic Enzyme Production and Gene Expression under Straw-State Cultivation inInternational journal of molecular sciences · 2023Article
- Enhancement of Inhibition of theInternational journal of molecular sciences · 2023Article
- Identification and characterization of a critical loop for the high activity of alginate lyase VaAly2 from the PL7_5 subfamily.Frontiers in microbiology · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alginate is a linear polysaccharide produced mainly by brown algae in marine environments. Alginate consists of a linear block copolymer made up of two monomeric units, β-d-mannuronate (M) and its C-5 epimer α-l-guluronate (G). Alginate lyases are polysaccharide lyases (PL) that degrade alginate via a β-elimination reaction. These enzymes play an important role in marine carbon recycling and also have widespread industrial applications. So far, more than 1,774 alginate lyase sequences have been identified and are distributed into 7 PL families. In this review, the folds, conformational changes during catalysis, and catalytic mechanisms of alginate lyases are described. Thus far, structures for 15 alginate lyases have been solved and are divided into 3 fold classes: the β-jelly roll class (PL7, -14, and -18), the (α/α)n toroid class (PL5, -15, and -17), and the β-helix fold (PL6). These enzymes adopt two different mechanisms for catalysis, and three kinds of conformational changes occur during this process. Moreover, common features in the structures, conformational changes, and catalytic mechanisms are summarized, providing a comprehensive understanding on alginate lyases.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.