C1-Cx revisited: intramolecular synergism in a cellulase.
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.
Din
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N
Department of Microbiology and Immunology, University of British Columbia, Vancouver, Canada.
Damude
H G
HG
Gilkes
N R
NR
Miller
R C
RC
Warren
R A
RA
Kilburn
D G
DG
D000192:Actinomycetales / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry; D002480:Cellulase / Q000737:chemistry*; D016297:Mutagenesis, Site-Directed; D011994:Recombinant Proteins; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D002480:Cellulase