C1-Cx revisited: intramolecular synergism in a cellulase.

N. Din, Howard G. Damude, Neil R. Gilkes, Robert C. Miller, R. A. J. Warren, Douglas G. Kilburn

Proceedings of the National Academy of Sciences · 1994 · 177 citations · 13 references

Concepts

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.

References

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