ArticleThe Journal of biological chemistry2019
The molecular basis of endolytic activity of a multidomain alginate lyase from
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.
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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.
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Who cites it
26 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Encapsulation of Saccharomyces spp. for Use as Probiotic in Food and Feed: Systematic Review and Meta-analysis.Probiotics and antimicrobial proteins · 2024Pooled it
- Structural and functional insights into Uly1040, an ulvan lyase from polysaccharide lyase family 40.Applied and environmental microbiology · 2026Article
- Article
- Structural and functional analysis of Pseudomonas aeruginosa PelA provides insight into the modification of the Pel exopolysaccharide.The Journal of biological chemistry · 2025Article
- Insights into the mechanism of substrate specificity in a novel PL15_3 subfamily oligo-alginate lyase VBAly15A.Applied and environmental microbiology · 2025Article
- Insights into putative alginate lyases from epipelagic and mesopelagic communities of the global ocean.Scientific reports · 2025Article
- Bacterial polysaccharide lyase family 33: Specificity from an evolutionarily conserved binding tunnel.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Alginate-Degrading Modes, Oligosaccharide-Yielding Properties, and Potential Applications of a Novel Bacterial Multifunctional Enzyme, Aly16-1.Microorganisms · 2024Article
- Pseudomonas aeruginosa biofilm exopolysaccharides: assembly, function, and degradation.FEMS microbiology reviews · 2023Review
- Article
- Identification and structural analysis of a carbohydrate-binding module specific to alginate, a representative of a new family, CBM96.The Journal of biological chemistry · 2023Article
- Prophage-Derived Regions inInternational journal of molecular sciences · 2023Article
- Synergy of the Two Alginate Lyase Domains of a Novel Alginate Lyase fromApplied and environmental microbiology · 2022Article
- Effects of Module Truncation of a New Alginate Lyase VxAly7C from MarineInternational journal of molecular sciences · 2022Article
- A Novel Alginate Lyase: Identification, Characterization, and Potential Application in Alginate Trisaccharide Preparation.Marine drugs · 2022Article
- Evolving strategies for marine enzyme engineering: recent advances on the molecular modification of alginate lyase.Marine life science & technology · 2022Review
- Towards Consistency in Geometry Restraints for Carbohydrates in the Pyranose form: Modern Dictionary Generators Reviewed.Current medicinal chemistry · 2022Article
- Enzymatic depolymerization of alginate by two novel thermostable alginate lyases fromFrontiers in plant science · 2022Article
- Structure-function analysis of a new PL17 oligoalginate lyase from the marine bacterium Zobellia galactanivorans DsijT.Glycobiology · 2021Article
- Structure Characteristics, Biochemical Properties, and Pharmaceutical Applications of Alginate Lyases.Marine drugs · 2021Review
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alginate is a polymer containing two uronic acid epimers, β-d-mannuronate (M) and α-l-guluronate (G), and is a major component of brown seaweed that is depolymerized by alginate lyases. These enzymes have diverse specificity, cleaving the chain with endo- or exotype activity and with differential selectivity for the sequence of M or G at the cleavage site. Dp0100 is a 201-kDa multimodular, broad-specificity endotype alginate lyase from the marine thermophile
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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.