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![[Figure 5]](jc5049fig5mag.jpg)
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Figure 5
Comparison of the activity of MtGlu5 and Trp mutants towards RAC. (a) Single to triple Trp mutations of MtCBM. In contrast to the WT, all Trp mutants of MtCBM show decreased glucanase activity. (b) The single amino-acid mutations in the putative binding groove of the catalytic domain, W43A, W188A and W224A, show dramatically decreased activity. However, the W192A and E216A mutants in the interactive surface between the CD and CBM display no significant difference. All activities are presented as relative activity (%) measured at optimum pH and temperature. Data are shown as the means ± SD of more than three replicates. **** indicates statistical significance at the p < 0.0001 level and ns represents no statistical significance compared with MtGlu5. (c) Enzyme activities of MtGlu5 towards various substrates. As the data show, MtGlu5 is highly specific for β-1,4-glucan, indicating that MtGlu5 belongs to EC 3.2.1.4. The specific activities of MtGlu5 towards CMC, β-glucan (barley) and cellopentaose are 385 ± 5, 1090 ± 210 and 56.5 ± 6.5 IU, respectively. |
![[Figure 5]](jc5049fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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