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![[Figure 3]](jc5049fig3mag.jpg)
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Figure 3
Functional and structural comparison among enzymes with or without an inserted MtCBM. (a) Comparison of the glucanase activity of MtGlu5 (WT) and ΔCBM towards regenerated amorphous cellulose (RAC). The specific activities of MtGlu5 and ΔCBM towards RAC are 4.24 ± 0.44 and 2.41 ± 0.24 IU, respectively. The activities are presented as relative activity (%) measured in optimum buffer consisting of 20 mM citrate/HEPES/CHES and 100 mM sodium chloride pH 5.0. Data are exhibited as the means ± SD of more than three replicates. *** indicates statistical significance at the p < 0.001 level compared with MtGlu5. (b) Comparison of the glucanase activity of wild-type TmCel5A and chimeric TmCel5A-CBM towards RAC under optimal conditions. The specific activities of TmCel5A and TmCel5A-CBM towards RAC are 1.57 ± 0.11 and 4.30 ± 0.10 IU, respectively. The activities are presented as the relative activity (%) measured under optimum conditions. Data are exhibited as the means ± SD of more than three replicates. **** indicates statistical significance at the p < 0.0001 level compared with TmCel5A. (c) Superimposition of the structures of MtGlu5 (dark blue; PDB entry 7vt8), ΔCBM (green cyan; PDB entry 7vt5) and TmCel5A (deep salmon; PDB entry 3mmu). Each catalytic domain of the three structures overlays well except for the α6 helix and the loop containing an important residue for substrate binding: Trp224 in MtGlu5 and ΔCBM (equivalent to Trp210 in TmCel5A). |
![[Figure 3]](jc5049fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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