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- W2085655506 abstract "The possible structural and catalytic functions of the nine tryptophan amino acid residues, including Trp54, Trp105, Trp112, Trp141, Trp148, Trp165, Trp186, Trp198, and Trp203 in Fibrobacter succinogenes 1,3−1,4-β-d-glucanase (Fsβ-glucanase), were characterized using site-directed mutagenesis, initial rate kinetics, fluorescence spectrometry, and structural modeling analysis. Kinetic studies showed that a 5−7-fold increase in Km value for lichenan was observed for W141F, W141H, and W203R mutant Fsβ-glucanases, and approximately 72-, 56-, 30-, 29.5-, 4.9-, and 4.3-fold decreases in kcat relative to that for the wild-type enzyme were observed for the W54F, W54Y, W141H, W203R, W141F, and W148F mutants, respectively. In contrast, W186F and W203F, unlike the other 12 mutants, exhibited a 1.4- and 4.2-fold increase in kcat, respectively. W165F and W203R were the only two mutants that exhibited a 4−7-fold higher activity relative to the wild-type enzyme after they were incubated at pH 3.0 for 1 h. Fluorescence spectrometry indicated that all of the mutations on the nine tryptophan amino acid residues retained a folding similar to that of the wild-type enzyme. Structural modeling and kinetic studies suggest that Trp54, Trp141, Trp148, and Trp203 play important roles in maintaining structural integrity in the substrate-binding cleft and the catalytic efficiency of the enzyme." @default.
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- W2085655506 date "2002-06-12" @default.
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- W2085655506 title "Mutagenesis of Trp<sup>54</sup> and Trp<sup>203</sup> Residues on <i>Fibrobacter Succinogenes </i>1,3−1,4-β-<scp>d</scp>-Glucanase Significantly Affects Catalytic Activities of the Enzyme" @default.
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- W2085655506 doi "https://doi.org/10.1021/bi025766l" @default.
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