Enzyme Functionality Design Engineering And by Allan Svendsen

By Allan Svendsen

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In: SB Petersen, B Svensson, S Petersen, eds. Carbohydrate Bioengineering. Amsterdam: Elsevier Science, 1995, pp 175–179. M Wyss, L Pasamontes, A Friedlein, R Re´my, M Tessier, A Kronenberger, A Middendorf, M Lehmann, L Schnoebelen, U Ro¨thlisberger, E Kusznir, G Wahl, F Mu¨ller, H-W Lahm, K Vogel, APGM van Loon. Biophysical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): molecular size, glycosylation pattern, and engineering of proteolytic resistance. Appl Environ Microbiol 65:367–373, 1999.

One single-point mutation doubled the enantioselectivity while another mutation annihilated the enantioselectivity toward the target substrate. However, as already mentioned for rational stability engineering, every amino acid substitution can cause adaptations of the entire protein structure to the introduction of a new amino acid residue. This can perturb or even reverse a predicted effect on the enzyme. 4 OUTLOOK Every amino acid substitution has a more or less pronounced effect on the entire structure of a protein, which means that most of the time its effect Concepts for Protein Engineering 11 reaches far beyond the actual site of mutation.

Optimization of the catalytic properties of Aspergillus fumigatus phytase based on the three-dimensional structure. Protein Sci 9: 1304–1311, 2000. C Cunningham, JA Wells. High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis. Science 244:1081–1085, 1989. TV Borchert, SF Lassen, A Svendsen, HB Frantzen. Oxidation stable amylases for detergents. In: SB Petersen, B Svensson, S Petersen, eds. Carbohydrate Bioengineering. Amsterdam: Elsevier Science, 1995, pp 175–179.

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