PMID:2043125
| Citation |
Murase, S, Takagi, JS, Higashi, Y, Imaishi, H, Yumoto, N and Tokushige, M (1991) Activation of aspartase by site-directed mutagenesis. Biochem. Biophys. Res. Commun. 177:414-9 |
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| Abstract |
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. |
| Links | |
| Keywords |
Amino Acid Sequence; Aspartate Ammonia-Lyase/genetics; Aspartate Ammonia-Lyase/metabolism; Circular Dichroism; Cysteine; Enzyme Activation; Escherichia coli/enzymology; Escherichia coli/genetics; Kinetics; Mutagenesis, Site-Directed; Peptide Fragments/isolation & purification; Protein Conformation; Tryptophan |
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