ArticleThe Journal of biological chemistry2014
Characterization of all family-9 glycoside hydrolases synthesized by the cellulosome-producing bacterium Clostridium cellulolyticum.
Article in The Journal of biological chemistry, 2014. 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.
- Improvement of arabinoxylan degradation in Clostridium saccharobutylicum DSM 13864Applied microbiology and biotechnology · 2025Article
- Uncovering enzymatic tools promoting lignocellulose breakdown in the anaerobic bacterium Ruminiclostridium cellulolyticum.Communications biology · 2025Article
- Genome-scale metabolic modeling ofmSystems · 2025Article
- A GTP-driven central carbon metabolism in the cellulolytic bacterium Ruminiclostridium cellulolyticum.Communications biology · 2025Article
- Combining transcriptomic and metabolomic insights into carbohydrate utilization by Ruminiclostridium papyrosolvens DSM2782.Biotechnology for biofuels and bioproducts · 2025Article
- Enzymatic degradation of cellulose in soil: A review.Heliyon · 2024Article
- The supragenic organization of glycoside hydrolase encoding genes reveals distinct strategies for carbohydrate utilization in bacteria.Frontiers in microbiology · 2023Article
- Insights into lignocellulose degradation: comparative genomics of anaerobic and cellulolyticFrontiers in microbiology · 2023Article
- Insight into CAZymes ofInternational journal of molecular sciences · 2022Article
- Selfish uptake versus extracellular arabinoxylan degradation in the primary degrader Ruminiclostridium cellulolyticum, a new string to its bow.Biotechnology for biofuels and bioproducts · 2022Article
- A processive GH9 family endoglucanase of Bacillus licheniformis and the role of its carbohydrate-binding domain.Applied microbiology and biotechnology · 2022Article
- Synergic action of an inserted carbohydrate-binding module in a glycoside hydrolase family 5 endoglucanase.Acta crystallographica. Section D, Structural biology · 2022Article
- Internal Transcription Terminators Control Stoichiometry of ABC Transporters in Cellulolytic Clostridia.Microbiology spectrum · 2022Article
- Article
- Some characters of bacterial cellulases in goats' rumen elucidated by metagenomic DNA analysis and the role of fibronectin 3 module for endoglucanase function.Animal bioscience · 2021Article
- Heterologous Expression of Lignocellulose-Modifying Enzymes in Microorganisms: Current Status.Molecular biotechnology · 2021Review
- Cellulosomes: Highly Efficient Cellulolytic Complexes.Sub-cellular biochemistry · 2021Review
- A Novel Two-Component System, XygS/XygR, Positively Regulates Xyloglucan Degradation, Import, and Catabolism in Ruminiclostridium cellulolyticum.Applied and environmental microbiology · 2020Article
- Function-driven single-cell genomics uncovers cellulose-degrading bacteria from the rare biosphere.The ISME journal · 2020Article
- A Cell-Surface GH9 Endo-Glucanase Coordinates with Surface Glycan-Binding Proteins to Mediate Xyloglucan Uptake in the Gut Symbiont Bacteroides ovatus.Journal of molecular biology · 2019Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The genome of Clostridium cellulolyticum encodes 13 GH9 enzymes that display seven distinct domain organizations. All but one contain a dockerin module and were formerly detected in the cellulosomes, but only three of them were previously studied (Cel9E, Cel9G, and Cel9M). In this study, the 10 uncharacterized GH9 enzymes were overproduced in Escherichia coli and purified, and their activity pattern was investigated in the free state or in cellulosome chimeras with key cellulosomal cellulases. The newly purified GH9 enzymes, including those that share similar organization, all exhibited distinct activity patterns, various binding capacities on cellulosic substrates, and different synergies with pivotal cellulases in mini-cellulosomes. Furthermore, one enzyme (Cel9X) was characterized as the first genuine endoxyloglucanase belonging to this family, with no activity on soluble and insoluble celluloses. Another GH9 enzyme (Cel9V), whose sequence is 78% identical to the cellulosomal cellulase Cel9E, was found inactive in the free and complexed states on all tested substrates. The sole noncellulosomal GH9 (Cel9W) is a cellulase displaying a broad substrate specificity, whose engineered form bearing a dockerin can act synergistically in minicomplexes. Finally, incorporation of all GH9 cellulases in trivalent cellulosome chimera containing Cel48F and Cel9G generated a mixture of heterogeneous mini-cellulosomes that exhibit more activity on crystalline cellulose than the best homogeneous tri-functional complex. Altogether, our data emphasize the importance of GH9 diversity in bacterial cellulosomes, confirm that Cel9G is the most synergistic GH9 with the major endoprocessive cellulase Cel48F, but also identify Cel9U as an important cellulosomal component during cellulose depolymerization.
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