N. Din et al., C-1-C-X REVISITED - INTRAMOLECULAR SYNERGISM IN A CELLULASE, Proceedings of the National Academy of Sciences of the United Statesof America, 91(24), 1994, pp. 11383-11387
Endoglucanase A (CenA) from the bacterium Cellulomonas fimi is compose
d of a catalytic domain and a nonhydrolytic cellulose-binding domain t
hat can function independently. The individual domains interact synerg
istically in the disruption and hydrolysis of cellulose fibers. This i
ntramolecular synergism is distinct from the well known intermolecular
synergism between individual cellulases. The catalytic domain corresp
onds to the hydrolytic C-X system and the cellulose-binding domain cor
responds to the nonhydrolytic C-1 system postulated by Reese et al. [R
eese, E. T., Sui, R. G. H. and Levinson, H. S. (1950) J. Bacteriol. 59
, 485-497] to be required for the hydrolysis of cellulose.