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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Enhancement of the stability and activity of aspartase by random and site-directed mutagenesis.

Enzymatic generation of mutant libraries for random mutagenesis of aspartase gene from E. coli J2 was made. A mutant enzyme with 4-fold increase in aspartase activity was found. It is stable at pH7.5-9.0 (wild-type: pH7.0-8.0); heat stability and alpha-helicity are higher than those of the wild-type. By using site directed mutagenesis, the aspartase was activated by replacement of Lys-126 with an arginine residue. The mutation produced functional alterations without appreciable structure changes. The optimum pH for the mutant enzyme is 8. 5. The stable pH range is 7.0-9. 0. Heat stability is higher than that of the wild-type one. Activity of the mutant enzyme is about 5-fold as much as that of wild-type one.[1]

References

  1. Enhancement of the stability and activity of aspartase by random and site-directed mutagenesis. Zhang, H.Y., Zhang, J., Lin, L., Du, W.Y., Lu, J. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
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