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Revision as of 23:53, 19 October 2011

CelD Mutated Cellulase

Clostridium thermocellum endoglucanase CelD is a representative enzyme for detailed structural and functional studies of the family E cellulases.
Beside C. thermocellum’s CelD, E family cellulases include a number of cellulases of bacterial, fungal, and plant origin.
CelD, has been previously overexpressed in Escherichia coli, the enzyme is easily purified in large amounts from cytoplasmic inclusion bodies. (Chauvaux, Beguin, Aubert, 1992)
The CelD sequence used has an aminoacid substitution Asp-523 ---> Ala. That mutation increases the specific activity of the enzyme by 224% (Chauvaux, Beguin, Aubert, 1992)

References

Chauvaux, S., Beguin, P., & Aubert, J. (1992). Site-directed mutagenesis of essential carboxylic residues in clostridium thermocellum endoglucanase celd*. The Journal of Biological Chemistry, 267(5), 4472-4478.

Sequence and Features