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Báo cáo Y học: The role of amino-acid residues Q39 and E451 in the determination of substrate specificity of the Spodoptera frugiperda b-glycosidase

Chia sẻ: Nguyễn Tuấn | Ngày: | Loại File: PDF | Số trang:10

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The design of b-glycosidases with planed substrate specificity for biotechnological application has received little attention. This is mostly a consequence of the lack of data on the molecular basis of the b-glycosidase specificity, namely data on the energy of the noncovalent interactions in the enzymetransition state complex. In an attempt to fill this gap, sitedirected mutagenesis and enzyme steady-state kinetic experiments with different substrates were conducted, using as model a digestive b-glycosidase (glycoside hydrolase family 1) from Spodoptera frugiperda (Lepidoptera) (Sfbgly50). The active site of this enzyme was modeled based on its sequence and on crystallographic data of similar enzymes....

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Nội dung Text: Báo cáo Y học: The role of amino-acid residues Q39 and E451 in the determination of substrate specificity of the Spodoptera frugiperda b-glycosidase

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