ArticleApplied and environmental microbiology2022
Discovery of a Novel Glucuronan Lyase System in
Article in Applied and environmental microbiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 23 citations in OpenAlex.
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- Discovery of a bacteriophage sequence in a mite genome assembly reveals bacterial contamination and opens new possibilities for exploring arthropod symbionts.Microbial genomics · 2025Article
- Insights into putative alginate lyases from epipelagic and mesopelagic communities of the global ocean.Scientific reports · 2025Article
- Carbohydrate-active enzymes from Akkermansia muciniphila break down mucin O-glycans to completion.Nature microbiology · 2025Article
- Discovery and Characterization of Mannan-Specialized GH5 Endo-1,4-β-mannanases: a Strategy for Açaí (Journal of agricultural and food chemistry · 2025Article
- Heterologous Expression and Characterization of Cellouronate (β-1,4-Glucuronan) Lyase from a Human Intestinal BacteriumJournal of applied glycoscience · 2025Article
- Three alginate lyases provide a new gutApplied and environmental microbiology · 2023Article
- Genome Analysis of a Novel Polysaccharide-Degrading BacteriumMarine drugs · 2022Article
- Degradation of Alginate by a Newly Isolated Marine BacteriumMarine drugs · 2022Article
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7 authors at 1 institution in 1 country.
Funding
Abstract
Glucuronan lyases (EC 4.2.2.14) catalyze depolymerization of linear β-(1,4)-polyglucuronic acid (glucuronan). Only a few glucuronan lyases have been characterized until now, most of them originating from bacteria. Here we report the discovery, recombinant production, and functional characterization of the full complement of six glucuronan specific polysaccharide lyases in the necrotic mycoparasite Trichoderma parareesei. The enzymes belong to four different polysaccharide lyase families and have different reaction optima and glucuronan degradation profiles. Four of them showed endo-lytic action and two, TpPL8A and TpPL38A, displayed exo-lytic action. Nuclear magnetic resonance revealed that the monomeric end product from TpPL8A and TpPL38A underwent spontaneous rearrangements to tautomeric forms. Proteomic analysis of the secretomes from T. parareesei growing on pure glucuronan and lyophilized A. bisporus fruiting bodies, respectively, showed secretion of five of the glucuronan lyases and high-performance anion-exchange chromatography with pulsed amperometric detection analysis confirmed the presence of glucuronic acid in the A. bisporus fruiting bodies. By systematic genome annotation of more than 100 fungal genomes and subsequent phylogenetic analysis of the putative glucuronan lyases, we show that glucuronan lyases occur in several ecological and taxonomic groups in the fungal kingdom. Our findings suggest that a diverse repertoire of glucuronan lyases is a common trait among Hypocreales species with mycoparasitic and entomopathogenic lifestyles.
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