Redesigning the Substrate Specificity of an Enzyme by Cumulative Effects of the Mutations of Non-active Site Residues
Directed evolution was used to change the substrate specificity of aspartate aminotransferase. A mutant enzyme with 17 amino acid substitutions was generated that shows a 2.1 x 10(6)-fold increase in the catalytic efficiency (kcat/Km) for a non-native substrate, valine. The absorption spectrum of th...
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| Hlavní autoři: | , , , |
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| Médium: | Artigo |
| Jazyk: | angličtina |
| Vydáno: |
1999
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| On-line přístup: | https://doi.org/10.1074/jbc.274.4.2344 http://www.jbc.org/article/S0021925819881838/pdf |
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