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EGIII,a new endoglucanase from Trichoderma reesei: the characterization of both gene and enzyme
Institution:1. Biotechnical Laboratory, VTT, SF-02150 Espoo Finland Tel. 358-0-4561;2. Institute of Biochemistry, University of Uppsala, Biomedical Center, UppsalaSweden Tel. 46-18-174000;3. Laboratory for Biochemistry, State University Ghent, Ghent Belgium Tel. 32-91-227821;1. Department of Biochemistry, Kirksville College of Osteopathic Medicine, A.T. Still University, Kirksville, MO, 63501, USA;2. Department of Anatomy, Kirksville College of Osteopathic Medicine, A.T. Still University, Kirksville, MO, 63501, USA;3. Department of Microbiology & Immunology, Kirksville College of Osteopathic Medicine, A.T. Still University, Kirksville, MO, 63501, USA;4. Faculty of Medicine, Cairo University, Cairo, Egypt;1. School of Bioengineering and Food Tehnology, Shoolini University, Solan 173212, H.P., India;2. Department of Biotechnology, Himachal Pradesh University, Shimla 171005, H.P., India;1. School of Life Science and Food Engineering, Huaiyin Institute of Technology, Huaian, Jiangsu, China;2. Jiangsu Provincial Engineering Laboratory for Biomass Conversion and Process Integration, Huaiyin Institute of Technology, Huaian, Jiangsu, China
Abstract:A novel endoglucanase from Trichoderma reesei, EGIII, has been purified and its catalytic properties have been studied. The gene for that enzyme (egl3) and cDNA have been cloned and sequenced. The deduced EGIII protein shows clear sequence homology to a Schizophyllum commune enzyme (M. Yaguchi, personal communication), but is very different from the three other T. reesei cellulases with known structure. Nevertheless, all the four T. reesei cellulases share two common, adjacent sequence domains, which apparently can be removed by proteolysis. These homologous sequences reside at the N termini of EGIII and the cellobiohydrolase CBHII, but at the C termini of EGI and CBHI. Comparison of the fungal cellulase structures has led to re-evaluation of hypotheses concerning the localization of the active sites.
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