Structural and functional modifications of a xylanase from Streptomyces lividans belonging to glycanase family 10
1996
Dupont, C. | Roberge, M. | Morosoli, R. | Shareck, F. | Moreau, A. | Kleupfel, D.
Site-directed mutagenesis in concert with kinetic characterization was used to investigate the role and function of highly conserved amino acid residues among xylanases of family 10 using xylanase A from Streptomyces lividans (XlnA). As an example, mutants with modified catalytic properties, thermostability and pH profile were obtained. The three-dimensional structure of XlnA was used to rationalize the effects of the mutations.
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