Abstract
Activity of a cellulosomal endoglucanase (endoglucanase E; EGE) from Clostridium thermocellum against two crystalline forms of cellulose was enhanced by combination with the cellulosome integrating protein (CipA), but CipA did not enhance EGE activity against amorphous cellulose, even though it was able to bind to it. Similarly, CipA added in trans to genetically truncated EGE that was unable to combine with it nevertheless enhanced EGE activity against crystalline cellulose. These results indicate that the CipA cellulose binding domain does not mediate an increase in activity solely by bringing the catalytic subunits of the cellulosome complex into intimate contact with the substrate.
Original language | English |
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Pages (from-to) | 221-224 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 422 |
Issue number | 2 |
DOIs | |
Publication status | Published - Jan 30 1998 |
Externally published | Yes |
Keywords
- Cellulase
- Cellulolysis
- Cellulosome
- Cellulosome integrating protein
- Clostridium thermocellum
- Endoglucanase E
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology