The tryptophan residue at the active site tunnel entrance of trichoderma reesei cellobiohydrolase Cel7A is Important for initiation of degradation of crystalline cellulose

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Abstract

Background: Mutation of Trp-40 in the Cel7A cellobiohydrolase from Trichoderma reesei (TrCel7A) causes a loss of crystalline cellulose-degrading ability. Results: Mutant W40A showed reduced specific activity for crystalline cellulose and diffused the cellulose chain from the entrance of the active site tunnel. Conclusion: Trp-40 is essential for chain end loading to initiate processive hydrolysis of TrCel7A. Significance: The mechanisms of crystalline polysaccharide degradation are clarified. Copyright © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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Nakamura, A., Tsukada, T., Auer, S., Furuta, T., Wada, M., Koivula, A., … Samejima, M. (2013). The tryptophan residue at the active site tunnel entrance of trichoderma reesei cellobiohydrolase Cel7A is Important for initiation of degradation of crystalline cellulose. Journal of Biological Chemistry, 288(19), 13503–13510. https://doi.org/10.1074/jbc.M113.452623

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