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Fig. 4 | BMC Biotechnology

Fig. 4

From: A trehalase from Zunongwangia sp.: characterization and improving catalytic efficiency by directed evolution

Fig. 4

a Location of amino acid substitutions in the predicted modules. The catalytic sites (Asp306, Glu494) and substitutions are in mutant C4. b The binding pocket superimposition of wild type (green color) and Y227H (red color). c The binding pocket of wild type (green color). d The binding pocket of Y227H (red color). e Docking analysis of TreZ-trehalose complex showing the position of trehalose in active cavity and the location of residue Arg442. f Docking analysis of R442G-trehalose complex showing the position of trehalose in active cavity and the location of residue Gly442

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