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Cel9M, a new family 9 cellulase of the Clostridium cellulolyticum cellulosome.
- Source :
-
Journal of bacteriology [J Bacteriol] 2002 Mar; Vol. 184 (5), pp. 1378-84. - Publication Year :
- 2002
-
Abstract
- A new cellulosomal protein from Clostridium cellulolyticum Cel9M was characterized. The protein contains a catalytic domain belonging to family 9 and a dockerin domain. Cel9M is active on carboxymethyl cellulose, and the hydrolysis of this substrate is accompanied by a decrease in viscosity. Cel9M has a slight, albeit significant, activity on both Avicel and bacterial microcrystalline cellulose, and the main soluble sugar released is cellotetraose. Saccharification of bacterial microcrystalline cellulose by Cel9M in association with two other family 9 enzymes from C. cellulolyticum, namely, Cel9E and Cel9G, was measured, and it was found that Cel9M acts synergistically with Cel9E. Complexation of Cel9M with the mini-CipC1 containing the cellulose binding domain, the X2 domain, and the first cohesin domain of the scaffoldin CipC of the bacterium did not significantly increase the hydrolysis of Avicel and bacterial microcrystalline cellulose.
- Subjects :
- Amino Acid Sequence
Bacterial Proteins chemistry
Bacterial Proteins genetics
Cellulase chemistry
Cellulase genetics
Clostridium genetics
Molecular Sequence Data
Recombinant Proteins genetics
Recombinant Proteins metabolism
Sequence Analysis, DNA
Bacterial Proteins classification
Bacterial Proteins metabolism
Carboxymethylcellulose Sodium metabolism
Cellulase classification
Cellulase metabolism
Clostridium enzymology
Organelles enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9193
- Volume :
- 184
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Journal of bacteriology
- Publication Type :
- Academic Journal
- Accession number :
- 11844767
- Full Text :
- https://doi.org/10.1128/JB.184.5.1378-1384.2002