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The biological degradation of cellulose.
The study of cellulolytic enzymes at the molecular level has revealed some of the features that contribute to their activity and an increasing number of three-dimensional structures are becoming available for cellulases and xylanases belonging to different families, which will provide paradigms for molecular modeling of related enzymes.
Molecular biology of cellulose degradation.
- P. Béguin
- BiologyAnnual review of microbiology
Detection of cellulase activity in polyacrylamide gels using Congo red-stained agar replicas.
- P. Béguin
- ChemistryAnalytical biochemistry
- 1 June 1983
Cloning of a Genetically Unstable Cytochrome P-450 Gene Cluster Involved in Degradation of the Pollutant Ethyltert-Butyl Ether by Rhodococcus ruber
Rhodococcus ruber IFP 2001 is one of a few bacterial strains able to degrade ethyl tert-butyl ether (ETBE), which is a major pollutant from gasoline, which was found to undergo a spontaneous 14.3-kbp chromosomal deletion, which results in the loss of the ability to degrade ETBE.
OlpB, a new outer layer protein of Clostridium thermocellum, and binding of its S-layer-like domains to components of the cell envelope
Results agree with the hypothesis that SLH domains contribute to the binding of exocellular proteins to the cell surface of bacteria.
A new type of cohesin domain that specifically binds the dockerin domain of the Clostridium thermocellum cellulosome-integrating protein CipA
A new type of cohesin domain, which is present in one, two, and four copies in SdbA, ORF2p, and OlpB, respectively, can be defined.
Cellulose-binding domains promote hydrolysis of different sites on crystalline cellulose.
- G. Carrard, A. Koivula, H. Söderlund, P. Béguin
- BiologyProceedings of the National Academy of Sciences…
- 12 September 2000
This interaction was used to study the effect of different cellulose-binding domains (CBDs) on the enzymatic activity of C. thermocellum endoglucanase CelD, proving the reversible binding of the intact complexes despite the apparent binding irreversibility of some CBDs.
Crystal structure and functional mapping of human ASMT, the last enzyme of the melatonin synthesis pathway
The X‐ray crystal structure of human N‐acetyl serotonin methyltransferase (ASMT), the last enzyme of the melatonin biosynthesis pathway, is presented and mapping of the variants on to the 3‐dimensional structure clarifies why some are harmful and provides a structural basis for understanding melatonin deficiency in humans.
The cellulosome: an exocellular, multiprotein complex specialized in cellulose degradation.
The architecture of the fungal complexes also seems to rely on the interaction of conserved, noncatalytic docking domains with a scaffolding component, suggesting that thefungal and clostridial complexes arose independently.
Organization of a Clostridium thermocellum gene cluster encoding the cellulosomal scaffolding protein CipA and a protein possibly involved in attachment of the cellulosome to the cell surface
Findings suggest that ORF3p might serve as an anchoring factor for the cellulosome on the cell surface by binding the duplicated segment that is present at the COOH end of CipA.