ArticleBiochemistry2012
Functional characterization of AlgL, an alginate lyase from Pseudomonas aeruginosa.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 45 citations in OpenAlex.
- Characterization of alginate-degrading bacteria isolated from seaweed-producing areas of South Korean territory and verification of the bacteria as plant growth-promoting biofertilizer.Microbiology spectrum · 2025Article
- Acyltransferases that Modify Cell Surface Polymers Across the Membrane.Biochemistry · 2025Review
- 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
- 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
- The RNA-Binding Protein ProQ Impacts Exopolysaccharide Biosynthesis and Second Messenger Cyclic di-GMP Signaling in the Fire Blight Pathogen Erwinia amylovora.Applied and environmental microbiology · 2022Article
- Comparison of Biochemical Characteristics, Action Models, and Enzymatic Mechanisms of a Novel Exolytic and Two Endolytic Lyases with Mannuronate Preference.Marine drugs · 2021Article
- Two New Alginate Lyases of PL7 and PL6 Families from Polysaccharide-Degrading BacteriumMarine drugs · 2020Article
- Structural and functional aspects of mannuronic acid-specific PL6 alginate lyase from the human gut microbeThe Journal of biological chemistry · 2019Article
- Structural and biochemical characterisation of a novel alginate lyase from Paenibacillus sp. str. FPU-7.Scientific reports · 2019Article
- Biochemical Characterization and Degradation Pattern of a Novel Endo-Type Bifunctional Alginate Lyase AlyA from Marine BacteriumMarine drugs · 2018Article
- Biochemical Characterization and Degradation Pattern of a Unique pH-Stable PolyM-Specific Alginate Lyase from Newly Isolated Serratia marcescens NJ-07.Marine drugs · 2018Article
- Characterization of a Long-Lived Alginate Lyase Derived from Shewanella Species YH1.Marine drugs · 2017Article
- One-step purification and characterization of alginate lyase fromIranian journal of basic medical sciences · 2017Article
- Biological function of a polysaccharide degrading enzyme in the periplasm.Scientific reports · 2016Article
- Biofilm dispersion in Pseudomonas aeruginosa.Journal of microbiology (Seoul, Korea) · 2016Review
- Engineering broad-spectrum digestion of polyuronides from an exolytic polysaccharide lyase.Biotechnology for biofuels · 2016Article
- Novel Alginate Lyase (Aly5) from a Polysaccharide-Degrading Marine Bacterium, Flammeovirga sp. Strain MY04: Effects of Module Truncation on Biochemical Characteristics, Alginate Degradation Patterns, and Oligosaccharide-Yielding Properties.Applied and environmental microbiology · 2016Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Alginate lyase (AlgL) catalyzes the cleavage of the polysaccharide alginate through a β-elimination reaction. In Pseudomonas aeruginosa, algL is part of the alginate biosynthetic operon, and although it is required for alginate biosynthesis, it is not clear why. Steady-state kinetic studies were performed to characterize its substrate specificity and revealed that AlgL operates preferentially on nonacetylated alginate or its precursor mannuronan. Mature alginate is secreted as a partially acetylated polysaccharide, so this observation is consistent with suggestions that AlgL serves to degrade mislocalized alginate that is trapped in the periplasmic space. The k(cat)/K(m) for the reaction increased linearly with the number of residues in the substrate, from 2.1 × 10(5) M(-1) s(-1) for the substrate containing 16 residues to 7.9 × 10(6) M(-1) s(-1) for the substrate with 280 residues. Over the same substrate size range, k(cat) varied between 10 and 30 s(-1). The variation in k(cat)/K(m) with substrate length suggests that AlgL operates in a processive manner. AlgL displayed a surprising lack of stereospecificity, in that it was able to catalyze cleavage adjacent to either mannuronate or guluronate residues in alginate. Thus, the enzyme is able to remove the C5 proton from both mannuronate and guluronate, which are C5 epimers. Exhaustive digestion of alginate by AlgL generated dimeric and trimeric products, which were characterized by (1)H nuclear magnetic resonance spectroscopy and mass spectrometry. Rapid-mixing chemical quench studies revealed that there was no lag in dimer or trimer production, indicating that AlgL operates as an exopolysaccharide lyase.
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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.