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Cellobiohydrolase A (CbhA) from the cellulolytic bacterium Cellulomonas fimi is a β-1,4-exoceilobiohydrolase analogous to Trichoderma reesei CBH II
Article first published online: 27 OCT 2006
DOI: 10.1111/j.1365-2958.1994.tb01030.x
1365-2958/asset/cover.gif?v=1&s=75254d9e3ae6a0f08085f34cc6e5bd65d8e3d52e "Molecular Microbiology")
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How to Cite
Meinke, A., Gilkes, N. R., Kwan, E., Kilburn, D. G., Warren, R. A. J. and Miller, R. C. (1994), Cellobiohydrolase A (CbhA) from the cellulolytic bacterium Cellulomonas fimi is a β-1,4-exoceilobiohydrolase analogous to Trichoderma reesei CBH II. Molecular Microbiology, 12: 413–422. doi: 10.1111/j.1365-2958.1994.tb01030.x
Publication History
- Issue published online: 27 OCT 2006
- Article first published online: 27 OCT 2006
- Received 28 October, 1993; revised 21 January, 1994; accepted 27 January, 1994.
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Summary
The gene cbhA from the cellulolytic bacterium Cellulomonas fimi encodes a protein of 872 amino acids designated cellobiohydrolase A (CbhA). Mature CbhA contains 832 amino acid residues and has a predicted molecular mass of 85 349 Da. It is composed of five domains: an N-terminal catalytic domain, three repeated sequences of 95 amino acids, and a C-terminal cellulose-binding domain typical of other C. fimi glycanases. The structure and enzymatic activities of the CbhA cataiytic domain are closely related to those of CBH ll, an exocelloblohydrolase in the glycosyl hydrolase family B from the fungus Trichoderma reesel. CbhA is the first such enzyme to be characterized in bacteria. The data support the proposal that extended loops around the active site distinguish exohydrolases from endohydrolases in this enzyme family.