ArticleJournal of bacteriology2003
Characterization of a cellulase containing a family 30 carbohydrate-binding module (CBM) derived from Clostridium thermocellum CelJ: importance of the CBM to cellulose hydrolysis.
Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 70 citations in OpenAlex.
- Dried tea residue can alter the blood metabolism and the composition and functionality of the intestinal microbiota in Hu sheep.Frontiers in microbiology · 2023Article
- The Function of CBM32 in Alginate Lyase VxAly7B on the Activity on Both Soluble Sodium Alginate and Alginate Gel.Frontiers in microbiology · 2021Article
- Carbohydrate Binding Modules: Diversity of Domain Architecture in Amylases and Cellulases From Filamentous Microorganisms.Frontiers in bioengineering and biotechnology · 2020Review
- Novel Endotype Xanthanase from Xanthan-DegradingApplied and environmental microbiology · 2019Article
- Article
- Mechanisms involved in xyloglucan catabolism by the cellulosome-producing bacterium Ruminiclostridium cellulolyticum.Scientific reports · 2016Article
- Article
- Characterization of all family-9 glycoside hydrolases synthesized by the cellulosome-producing bacterium Clostridium cellulolyticum.The Journal of biological chemistry · 2014Article
- Influence of a mannan binding family 32 carbohydrate binding module on the activity of the appended mannanase.Applied and environmental microbiology · 2012Article
- Characterization of Paenibacillus curdlanolyticus B-6 Xyn10D, a xylanase that contains a family 3 carbohydrate-binding module.Applied and environmental microbiology · 2011Article
- GASdb: a large-scale and comparative exploration database of glycosyl hydrolysis systems.BMC microbiology · 2010Article
- Isolation and identification of cellulose-binding proteins from sheep rumen contents.Applied and environmental microbiology · 2009Article
- Outer membrane proteins of Fibrobacter succinogenes with potential roles in adhesion to cellulose and in cellulose digestion.Journal of bacteriology · 2007Article
- Effect of the cellulose-binding domain on the catalytic activity of a beta-glucosidase from Saccharomycopsis fibuligera.Journal of industrial microbiology & biotechnology · 2007Article
- Essentiality of a newly identified carbohydrate-binding module for the function of CelB (BH0603) from the alkaliphilic bacterium Bacillus halodurans.Applied and environmental microbiology · 2006Article
- Cloning, sequencing, and expression of a Eubacterium cellulosolvens 5 gene encoding an endoglucanase (Cel5A) with novel carbohydrate-binding modules, and properties of Cel5A.Applied and environmental microbiology · 2005Article
- Cellulase, clostridia, and ethanol.Microbiology and molecular biology reviews : MMBR · 2005Review
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Clostridium thermocellum CelJ is a modular enzyme containing a family 30 carbohydrate-binding module (CBM) and a family 9 catalytic module at its N-terminal moiety. To investigate the functions of the CBM and the catalytic module, truncated derivatives of CelJ were constructed and characterized. Isothermal titration calorimetric studies showed that the association constants (K(a)) of the CBM polypeptide (CBM30) for the binding of cellopentaose and cellohexaose were 1.2 x 10(4) and 6.4 x 10(4) M(-1), respectively, and that the binding of CBM30 to these ligands is enthalpically driven. Qualitative analyses showed that CBM30 had strong affinity for cellulose and beta-1,3-1,4-mixed glucan such as barley beta-glucan and lichenan. Analyses of the hydrolytic action of the enzyme comprising the CBM and the catalytic module showed that the enzyme is a processive endoglucanse with strong activity towards carboxymethylcellulose, barley beta-glucan and lichenan. By contrast, the catalytic module polypeptide devoid of the CBM showed negligible activity toward these substrates. These observations suggest that the CBM is extremely important not only because it mediates the binding of the enzyme to the substrates but also because it participates in the catalytic function of the enzyme or contributes to maintaining the correct tertiary structure of the family 9 catalytic module for expressing enzyme activity.
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