ArticleThe Journal of biological chemistry2020
The hydrolysis mechanism of a GH45 cellulase and its potential relation to lytic transglycosylase and expansin function.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 29 citations in OpenAlex.
- A single-domain expansin-like protein fromProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Identification of QTLs and new candidate genes affecting ear shank length via BSA-seq and transcriptomic analysis in maize.Frontiers in plant science · 2026Article
- Lignocellulose degradation in bacteria and fungi: cellulosomes and industrial relevance.Frontiers in microbiology · 2025Review
- Genomic evidence for the widespread presence of GH45 cellulases among soil invertebrates.Molecular ecology · 2024Article
- The reaction mechanism of the Ideonella sakaiensis PETase enzyme.Communications chemistry · 2024Article
- The first crystal structure of a family 45 glycoside hydrolase from a brown-rot fungus, Gloeophyllum trabeum GtCel45A.FEBS open bio · 2024Article
- A trimeric glycosylated GH45 cellulase from the red abalone (Haliotis rufescens) exhibits endo and exoactivity.PloS one · 2024Article
- Loosenin-Like Proteins fromApplied and environmental microbiology · 2023Article
- In vitro studies of the protein-interaction network of cell-wall lytic transglycosylase RlpA of Pseudomonas aeruginosa.Communications biology · 2022Article
- Perspective: Path Sampling Methods Applied to Enzymatic Catalysis.Journal of chemical theory and computation · 2022Review
- Reconstructing reactivity in dynamic host-guest systems at atomistic resolution: amide hydrolysis under confinement in the cavity of a coordination cage.Chemical science · 2022Article
- QM/MM Simulations of Enzymatic Hydrolysis of Cellulose: Probing the Viability of an Endocyclic Mechanism for an Inverting Cellulase.Journal of chemical information and modeling · 2021Article
- A Swollenin FromFrontiers in microbiology · 2021Article
- Non-enzymatic action of expansins.The Journal of biological chemistry · 2020Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Family 45 glycoside hydrolases (GH45) are endoglucanases that are integral to cellulolytic secretomes, and their ability to break down cellulose has been successfully exploited in textile and detergent industries. In addition to their industrial relevance, understanding the molecular mechanism of GH45-catalyzed hydrolysis is of fundamental importance because of their structural similarity to cell wall-modifying enzymes such as bacterial lytic transglycosylases (LTs) and expansins present in bacteria, plants, and fungi. Our understanding of the catalytic itinerary of GH45s has been incomplete because a crystal structure with substrate spanning the -1 to +1 subsites is currently lacking. Here we constructed and validated a putative Michaelis complex
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