ArticleProceedings of the National Academy of Sciences of the United States of America2013
Structural characterization of a unique marine animal family 7 cellobiohydrolase suggests a mechanism of cellulase salt tolerance.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 104 citations in OpenAlex.
- A review of the historic and present ecological role of aquatic and shoreline wood, from forest to deep sea.Biological reviews of the Cambridge Philosophical Society · 2026Review
- Characterization of a novel halophilic and thermostable multifunctional cellulase from Ebinur Salt Lake.Scientific reports · 2025Article
- Genomic evidence for the widespread presence of GH45 cellulases among soil invertebrates.Molecular ecology · 2024Article
- Functional characterisation of a new halotolerant seawater active glycoside hydrolase family 6 cellobiohydrolase from a salt marsh.Scientific reports · 2024Article
- Salt-tolerant and thermostable mechanisms of an endoglucanase from marine Aspergillus niger.Bioresources and bioprocessing · 2022Article
- De novo transcriptome assembly of the midgut glands of herbivorous land crabs, Chiromantes haematocheir, and identification of laccase genes involved in lignin degradation.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2022Article
- Biochemical and Structural Analysis of a Glucose-Tolerant β-Glucosidase from the Hemicellulose-DegradingMolecules (Basel, Switzerland) · 2022Article
- Bacterial and fungal gut microbiota of supralittoral talitrid amphipods feeding on brown macroalgae and paper.PloS one · 2022Article
- Discovery of novel carbohydrate degrading enzymes from soda lakes through functional metagenomics.Frontiers in microbiology · 2022Article
- A Case Study of the Glycoside Hydrolase Enzyme Mechanism Using an Automated QM-Cluster Model Building Toolkit.Frontiers in chemistry · 2022Article
- Machine learning reveals sequence-function relationships in family 7 glycoside hydrolases.The Journal of biological chemistry · 2021Article
- Screening New Xylanase Biocatalysts from the Mangrove Soil Diversity.Microorganisms · 2021Article
- Exploring the Diversity of Fungal DyPs in Mangrove Soils to Produce and Characterize Novel Biocatalysts.Journal of fungi (Basel, Switzerland) · 2021Article
- Article
- Enzyme Properties of a Laccase Obtained from the Transcriptome of the Marine-Derived FungusInternational journal of molecular sciences · 2020Article
- Characterization of the CAZy Repertoire from the Marine-Derived FungusMarine drugs · 2020Article
- Engineering of a highly thermostable endoglucanase from the GH7 family of Bipolaris sorokiniana for higher catalytic efficiency.Applied microbiology and biotechnology · 2020Article
- To the Land and Beyond: Crab Microbiomes as a Paradigm for the Evolution of Terrestrialization.Frontiers in microbiology · 2020Review
- Isopod holobionts as promising models for lignocellulose degradation.Biotechnology for biofuels · 2020Article
- Lignocellulose degradation in isopods: new insights into the adaptation to terrestrial life.BMC genomics · 2019Article
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Authors and funding
15 authors at 5 institutions in 3 countries.
Funding
Abstract
Nature uses a diversity of glycoside hydrolase (GH) enzymes to convert polysaccharides to sugars. As lignocellulosic biomass deconstruction for biofuel production remains costly, natural GH diversity offers a starting point for developing industrial enzymes, and fungal GH family 7 (GH7) cellobiohydrolases, in particular, provide significant hydrolytic potential in industrial mixtures. Recently, GH7 enzymes have been found in other kingdoms of life besides fungi, including in animals and protists. Here, we describe the in vivo spatial expression distribution, properties, and structure of a unique endogenous GH7 cellulase from an animal, the marine wood borer Limnoria quadripunctata (LqCel7B). RT-quantitative PCR and Western blot studies show that LqCel7B is expressed in the hepatopancreas and secreted into the gut for wood degradation. We produced recombinant LqCel7B, with which we demonstrate that LqCel7B is a cellobiohydrolase and obtained four high-resolution crystal structures. Based on a crystallographic and computational comparison of LqCel7B to the well-characterized Hypocrea jecorina GH7 cellobiohydrolase, LqCel7B exhibits an extended substrate-binding motif at the tunnel entrance, which may aid in substrate acquisition and processivity. Interestingly, LqCel7B exhibits striking surface charges relative to fungal GH7 enzymes, which likely results from evolution in marine environments. We demonstrate that LqCel7B stability and activity remain unchanged, or increase at high salt concentration, and that the L. quadripunctata GH mixture generally contains cellulolytic enzymes with highly acidic surface charge compared with enzymes derived from terrestrial microbes. Overall, this study suggests that marine cellulases offer significant potential for utilization in high-solids industrial biomass conversion processes.
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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.