Din N, Damude H G, Gilkes N R, Miller R C, Warren R A, Kilburn D G
Department of Microbiology and Immunology, University of British Columbia, Vancouver, Canada.
Proc Natl Acad Sci U S A. 1994 Nov 22;91(24):11383-7. doi: 10.1073/pnas.91.24.11383.
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.
来自纤维单胞菌的内切葡聚糖酶A（CenA）由一个催化结构域和一个可独立发挥作用的非水解性纤维素结合结构域组成。在纤维素纤维的破坏和水解过程中，各个结构域协同发挥作用。这种分子内协同作用不同于单个纤维素酶之间众所周知的分子间协同作用。催化结构域对应于水解性的Cx系统，而纤维素结合结构域对应于里斯等人[里斯，E.T.，隋，R.G.H.和莱文森，H.S.（1950年）《细菌学杂志》59，485 - 497]推测的纤维素水解所需的非水解性C1系统。
