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. 1994 Nov 22;91(24):11383-7.
doi: 10.1073/pnas.91.24.11383.

C1-Cx revisited: intramolecular synergism in a cellulase

N Din  1 , H G Damude, N R Gilkes, R C Miller Jr, R A Warren, D G Kilburn
Affiliations

C1-Cx revisited: intramolecular synergism in a cellulase

N Din et al. Proc Natl Acad Sci U S A. .

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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