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![[Figure 6]](jc5037fig6mag.jpg)
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Figure 6
Active-site mutational design. (a) Sequence alignment of the catalytic domains of four GH20 enzymes: VhGlcNAcase, SpHex, SmChb and OfHex. Their amino-acid sequences were retrieved from the PDB using the PDB codes presented in Fig. 5 ![[link]](../../../../../../logos/arrows/d_arr.gif) . The sequence alignment was carried out by Clustal Omega (https://www.ebi.ac.uk/Tools/msa/clustalo/) and displayed by Jalview version 2.11.1.3 (https://www.jalview.org/). The conserved polar residues equivalent to Asp303, Asp304, His373, Asp437, Asp438 and Glu584 of VhGlcNAcase are shaded red, while the conserved aromatic residues equivalent to Trp487, Trp505, Tyr530, Trp546 and Trp582 are shaded blue. (b) The positions of the mutated residues Asp303, His373, Asp437, Asp438 and Glu584 in the catalytic pocket surrounding the −1 GlcNAc molecule. Colors: green for C atoms of the binding residues and black for the C atoms of the sugar molecule, blue for N atoms and red for O atoms. (c) Bar graphs representing the relative enzymatic activity of the active-site mutants in pNP-GlcNAc hydrolysis in comparison of that of WT VhGlcNAcase. |
![[Figure 6]](jc5037fig6.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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