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C1-Cx revisited: intramolecular synergism in a cellulase.

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Din, N, Damude, H G, Gilkes, N R, Miller, R C, Warren, R A, Kilburn, D G·1994·Proceedings of the National Academy of Sciences

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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Metadata

Authors
Din, N., Damude, H. G., Gilkes, N. R., Miller, R. C., Warren, R. A., & Kilburn, D. G.
Venue
Proceedings of the National Academy of Sciences
Published
1994-11-22
Volume
91
Issue
24
Pages
11383-11387
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2012232456
Cited by
178
References
0
FWCI
6.64
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: C1-Cx revisited: intramolecular synergism in a cellulase. https://app.cochat.ai/papers/10.1073/pnas.91.24.11383
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Din, N., Damude, H. G., Gilkes, N. R., Miller, R. C., Warren, R. A., & Kilburn, D. G. (1994). C1-Cx revisited: intramolecular synergism in a cellulase. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.91.24.11383

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