C1-Cx revisited: intramolecular synergism in a cellulase. |
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| Authors: | N Din H G Damude N R Gilkes R C Miller Jr R A Warren and D G Kilburn |
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| Affiliation: | Department of Microbiology and Immunology, University of British Columbia, Vancouver, Canada. |
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| Abstract: | Endoglucanase A (CenA) from the bacterium Cellulomonas fimi is composed of a catalytic domain and a nonhydrolytic cellulose-binding domain that can function independently. The individual domains interact synergistically in the disruption and hydrolysis of cellulose fibers. This intramolecular synergism is distinct from the well-known intermolecular synergism between individual cellulases. The catalytic domain corresponds to the hydrolytic Cx system and the cellulose-binding domain corresponds to the nonhydrolytic C1 system postulated by Reese et al. Reese, E. T., Sui, R. G. H. & Levinson, H. S. (1950) J. Bacteriol. 59, 485-497] to be required for the hydrolysis of cellulose. |
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