期刊
BIOTECHNOLOGY AND BIOENGINEERING
卷 113, 期 9, 页码 1873-1880出版社
WILEY-BLACKWELL
DOI: 10.1002/bit.25970
关键词
Cel7B; Trichoderma reesei; processivity; free energy calculations
资金
- National Natural Science Foundation of China [21173247, 31270785, 31400061]
- Qingdao Institute of Bioenergy and Bioprocess Technology Director Innovation Foundation [QIBEBT-DIFYS-201504]
Processivity is essential for cellulases in their catalysis of cellulose hydrolysis. But what drives the processive move is not well understood. In this work, we use Trichoderma reesei Cel7B as a model system and show that its processivity is directly correlated to the binding free energy difference of a cellulose chain occupying the binding sites -7 to +2 and that occupying sites -7 to -1. Several mutants that have stronger interactions with glycosyl units in sites +1 and +2 than the wild type enzyme show higher processivity. The results suggest that after the release of the product cellobiose located in sites +1 and +2, the enzyme pulls the cellulose chain to fill the vacant sites, which propels its processive move on the cellulose surface. (C) 2016 Wiley Periodicals, Inc.
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