Open AccessC1-Cx revisited: intramolecular synergism in a cellulase.
Author(s) -
Neena Din,
Howard G. Damude,
Neil R. Gilkes,
Robert C. Miller,
R. A. J. Warren,
Douglas G. Kilburn
Publication year - 1994
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.91.24.11383
Subject(s) - cellulase , cellulose , hydrolysis , intramolecular force , chemistry , catalysis , intermolecular force , domain (mathematical analysis) , stereochemistry , biochemistry , organic chemistry , molecule , mathematical analysis , mathematics
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.