Article
Conversion of aspartate aminotransferase into an L-aspartate beta-decarboxylase by a triple active-site mutation.
The Journal of biological chemistry - 29 Oct 1999
Graber R, Kasper P, Malashkevich V N, Strop P, Gehring H, Jansonius J N, Christen P
Abstract excerpt
The conjoint substitution of three active-site residues in aspartate aminotransferase (AspAT) of Escherichia coli (Y225R/R292K/R386A) increases the ratio of L-aspartate beta-decarboxylase activity to transaminase activity >25 million-fold. This result was achieved by combining an arginine shift mutation (Y225R/R386A) with a conservative substitution of a substrate-binding residue (R292K). In the wild-type enzyme,...
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