ArticleThe Journal of biological chemistry2012
Sequence, structure, and evolution of cellulases in glycoside hydrolase family 48.
Article in The Journal of biological chemistry, 2012. 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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Who cites it
14 citing papers in PubMed, 44 citations in OpenAlex.
- In Silico Study of Potential Binding Sites of the Family GH126 Enzyme CPF_2247 fromMolecules (Basel, Switzerland) · 2026Article
- From Waste to Wealth: Unlocking the Potential of Cellulase Characteristics for Food Processing Waste Management.Foods (Basel, Switzerland) · 2025Review
- Article
- Experimental and computational studies of cellulases as bioethanol enzymes.Bioengineered · 2022Review
- A Novel Primer Mixture for GH48 Genes: Quantification and Identification of Truly Cellulolytic Bacteria in Biogas Fermenters.Microorganisms · 2020Article
- Isolation and Characterization of Bacterial Cellulase Producers for Biomass Deconstruction: A Microbiology Laboratory Course.Journal of microbiology & biology education · 2019Article
- Natural diversity of glycoside hydrolase family 48 exoglucanases: insights from structure.Biotechnology for biofuels · 2017Article
- Horizontal Gene Transfer Contributes to the Evolution of Arthropod Herbivory.Genome biology and evolution · 2016Article
- Natural diversity of cellulases, xylanases, and chitinases in bacteria.Biotechnology for biofuels · 2016Article
- Production of a functional cell wall-anchored minicellulosome by recombinant Clostridium acetobutylicum ATCC 824.Biotechnology for biofuels · 2016Article
- Structures of exoglucanase from Clostridium cellulovorans: cellotetraose binding and cleavage.Acta crystallographica. Section F, Structural biology communications · 2015Article
- C/N ratio drives soil actinobacterial cellobiohydrolase gene diversity.Applied and environmental microbiology · 2015Article
- Metatranscriptomic analyses of plant cell wall polysaccharide degradation by microorganisms in the cow rumen.Applied and environmental microbiology · 2015Article
- Molecular Dynamics and Metadynamics Simulations of the Cellulase Cel48F.Enzyme research · 2014Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Currently, the cost of cellulase enzymes remains a key economic impediment to commercialization of biofuels. Enzymes from glycoside hydrolase family 48 (GH48) are a critical component of numerous natural lignocellulose-degrading systems. Although computational mining of large genomic data sets is a promising new approach for identifying novel cellulolytic activities, current computational methods are unable to distinguish between cellulases and enzymes with different substrate specificities that belong to the same protein family. We show that by using a robust computational approach supported by experimental studies, cellulases and non-cellulases can be effectively identified within a given protein family. Phylogenetic analysis of GH48 showed non-monophyletic distribution, an indication of horizontal gene transfer. Enzymatic function of GH48 proteins coded by horizontally transferred genes was verified experimentally, which confirmed that these proteins are cellulases. Computational and structural studies of GH48 enzymes identified structural elements that define cellulases and can be used to computationally distinguish them from non-cellulases. We propose that the structural element that can be used for in silico discrimination between cellulases and non-cellulases belonging to GH48 is an ω-loop located on the surface of the molecule and characterized by highly conserved rare amino acids. These markers were used to screen metagenomics data for "true" cellulases.
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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.