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

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Activation of aspartase by site-directed mutagenesis.

To elucidate the role of sulfhydryl groups in the enzymatic reaction of the aspartase from Escherichia coli, we used site-directed mutagenesis which showed that the enzyme was activated by replacement of Cys-430 with a tryptophan. This mutation produced functional alterations without appreciable structural change: The kcat values became 3-fold at pH 6.0; the Hill coefficient values became higher under both pH conditions; the dependence of enzyme activity on divalent metal ions increased; and hydroxylamine, a good substrate for the wild-type enzyme, proved a poor substrate for the mutant.[1]

References

  1. Activation of aspartase by site-directed mutagenesis. Murase, S., Takagi, J.S., Higashi, Y., Imaishi, H., Yumoto, N., Tokushige, M. Biochem. Biophys. Res. Commun. (1991) [Pubmed]
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