ArticleProceedings of the National Academy of Sciences of the United States of America2002
Convergent evolution sheds light on the anti-beta -elimination mechanism common to family 1 and 10 polysaccharide lyases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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30 citing papers in PubMed, 108 citations in OpenAlex.
- Crystal structure ofProceedings of the National Academy of Sciences of the United States of America · 2026Article
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- Unraveling the molecular mechanism of polysaccharide lyases for efficient alginate degradation.Nature communications · 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
- Insight into biodiversity of the recently rearranged genusFrontiers in plant science · 2023Article
- Pectinolytic lyases: a comprehensive review of sources, category, property, structure, and catalytic mechanism of pectate lyases and pectin lyases.Bioresources and bioprocessing · 2021Review
- Bacterial inducible expression of plant cell wall-binding protein YesO through conflict between Glycine max and saprophytic Bacillus subtilis.Scientific reports · 2020Article
- Enzymatic degradation of plant biomass and synthetic polymers.Nature reviews. Chemistry · 2020Review
- Structural and biochemical characterisation of a novel alginate lyase from Paenibacillus sp. str. FPU-7.Scientific reports · 2019Article
- Structural and functional analyses of glycoside hydrolase 138 enzymes targeting chain A galacturonic acid in the complex pectin rhamnogalacturonan II.The Journal of biological chemistry · 2019Article
- Screening of a Novel Polysaccharide Lyase Family 10 Pectate Lyase fromMolecules (Basel, Switzerland) · 2018Article
- Periplasmic depolymerase provides insight into ABC transporter-dependent secretion of bacterial capsular polysaccharides.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Diversity of Three-Dimensional Structures and Catalytic Mechanisms of Alginate Lyases.Applied and environmental microbiology · 2018Review
- Biochemical characterization of a novel ulvan lyase fromRSC advances · 2018Article
- An evolutionarily distinct family of polysaccharide lyases removes rhamnose capping of complex arabinogalactan proteins.The Journal of biological chemistry · 2017Article
- Functional Analyses of Resurrected and Contemporary Enzymes Illuminate an Evolutionary Path for the Emergence of Exolysis in Polysaccharide Lyase Family 2.The Journal of biological chemistry · 2015Article
- Chemical rescue and inhibition studies to determine the role of Arg301 in phosphite dehydrogenase.PloS one · 2014Article
- The power of two: arginine 51 and arginine 239* from a neighboring subunit are essential for catalysis in α-amino-β-carboxymuconate-epsilon-semialdehyde decarboxylase.The Journal of biological chemistry · 2013Article
- Article
- Investigation of the role of Arg301 identified in the X-ray structure of phosphite dehydrogenase.Biochemistry · 2012Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Enzyme-catalyzed beta-elimination of sugar uronic acids, exemplified by the degradation of plant cell wall pectins, plays an important role in a wide spectrum of biological processes ranging from the recycling of plant biomass through to pathogen virulence. The three-dimensional crystal structure of the catalytic module of a "family PL-10" polysaccharide lyase, Pel10Acm from Cellvibrio japonicus, solved at a resolution of 1.3 A, reveals a new polysaccharide lyase fold and is the first example of a polygalacturonic acid lyase that does not exhibit the "parallel beta-helix" topology. The "Michaelis" complex of an inactive mutant in association with the substrate trigalacturonate/Ca2+ reveals the catalytic machinery harnessed by this polygalacturonate lyase, which displays a stunning resemblance, presumably through convergent evolution, to the tetragalacturonic acid complex observed for a structurally unrelated polygalacturonate lyase from family PL-1. Common coordination of the -1 and +1 subsite saccharide carboxylate groups by a protein-liganded Ca2+ ion, the positioning of an arginine catalytic base in close proximity to the alpha-carbon hydrogen and numerous other conserved enzyme-substrate interactions, considered in light of mutagenesis data for both families, suggest a generic polysaccharide anti-beta-elimination mechanism.
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