ArticleJournal of bacteriology2000
CelE, a multidomain cellulase from Clostridium cellulolyticum: a key enzyme in the cellulosome?
Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 77 citations in OpenAlex.
- A processive GH9 family endoglucanase of Bacillus licheniformis and the role of its carbohydrate-binding domain.Applied microbiology and biotechnology · 2022Article
- Intein-mediated assembly of tunable scaffoldins for facile synthesis of designer cellulosomes.Applied microbiology and biotechnology · 2018Article
- Multiple cellobiohydrolases and cellobiose phosphorylases cooperate in the ruminal bacterium Ruminococcus albus 8 to degrade cellooligosaccharides.Scientific reports · 2016Article
- Mechanisms involved in xyloglucan catabolism by the cellulosome-producing bacterium Ruminiclostridium cellulolyticum.Scientific reports · 2016Article
- Synergistic properties of cellulases from Clostridium cellulovorans in the presence of cellobiose.AMB Express · 2016Article
- Screening and characterization of amylase and cellulase activities in psychrotolerant yeasts.BMC microbiology · 2016Article
- CenC, a multidomain thermostable GH9 processive endoglucanase from Clostridium thermocellum: cloning, characterization and saccharification studies.World journal of microbiology & biotechnology · 2015Article
- Combining free and aggregated cellulolytic systems in the cellulosome-producing bacterium Ruminiclostridium cellulolyticum.Biotechnology for biofuels · 2015Article
- Characterization of all family-9 glycoside hydrolases synthesized by the cellulosome-producing bacterium Clostridium cellulolyticum.The Journal of biological chemistry · 2014Article
- Self-surface assembly of cellulosomes with two miniscaffoldins on Saccharomyces cerevisiae for cellulosic ethanol production.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Scaffoldin modules serving as "cargo" domains to promote the secretion of heterologous cellulosomal cellulases by Clostridium acetobutylicum.Applied and environmental microbiology · 2011Article
- The issue of secretion in heterologous expression of Clostridium cellulolyticum cellulase-encoding genes in Clostridium acetobutylicum ATCC 824.Applied and environmental microbiology · 2011Article
- Surface display of a functional minicellulosome by intracellular complementation using a synthetic yeast consortium and its application to cellulose hydrolysis and ethanol production.Applied and environmental microbiology · 2010Article
- Molecular and microscopical investigation of the microflora inhabiting a deteriorated Italian manuscript dated from the thirteenth century.Microbial ecology · 2010Article
- Functional assembly of minicellulosomes on the Saccharomyces cerevisiae cell surface for cellulose hydrolysis and ethanol production.Applied and environmental microbiology · 2009Article
- Incorporation of fungal cellulases in bacterial minicellulosomes yields viable, synergistically acting cellulolytic complexes.Applied and environmental microbiology · 2007Article
- Transcriptional analysis of the cip-cel gene cluster from Clostridium cellulolyticum.Journal of bacteriology · 2006Article
- Characterization and gene cloning of a cold-active cellulase from a deep-sea psychrotrophic bacterium Pseudoalteromonas sp. DY3.Extremophiles : life under extreme conditions · 2006Article
- Molecular cloning and transcriptional and expression analysis of engO, encoding a new noncellulosomal family 9 enzyme, from Clostridium cellulovorans.Journal of bacteriology · 2005Article
- Cellulase, clostridia, and ethanol.Microbiology and molecular biology reviews : MMBR · 2005Review
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CelE, one of the three major proteins of the cellulosome of Clostridium cellulolyticum, was characterized. The amino acid sequence of the protein deduced from celE DNA sequence led us to the supposition that CelE is a three-domain protein. Recombinant CelE and a truncated form deleted of the putative cellulose binding domain (CBD) were obtained. Deletion of the CBD induces a total loss of activity. Exhibiting rather low levels of activity on soluble, amorphous, and crystalline celluloses, CelE is more active on p-nitrophenyl-cellobiose than the other cellulases from this organism characterized to date. The main product of its action on Avicel is cellobiose (more than 90% of the soluble sugars released), and its attack on carboxymethyl cellulose is accompanied by a relatively small decrease in viscosity. All of these features suggest that CelE is a cellobiohydrolase which has retained a certain capacity for random attack mode. We measured saccharification of Avicel and bacterial microcrystalline cellulose by associations of CelE with four other cellulases from C. cellulolyticum and found that CelE acts synergistically with all tested enzymes. The positive influence of CelE activity on the activities of other cellulosomal enzymes may explain its relative abundance in the cellulosome.
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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.