Publication: Conversion of aspartate aminotransferase into an L-aspartate beta-decarboxylase by a triple active-site mutation
Conversion of aspartate aminotransferase into an L-aspartate beta-decarboxylase by a triple active-site mutation
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Graber, R., Kasper, P., Malashkevich, V. N., Strop, P., Gehring, H., Jansonius, J. N., & Christen, P. (1999). Conversion of aspartate aminotransferase into an L-aspartate beta-decarboxylase by a triple active-site mutation. Journal of Biological Chemistry, 274(44), 31203–31325. https://doi.org/10.1074/jbc.274.44.31203
Abstract
Abstract
Abstract
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, Arg(386) interacts with the alpha-carboxylate group of the substrate and is one of the four residues that are invariant in
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Creators (Authors)
- Graber, R
- Kasper, P
- Malashkevich, V N
- Strop, P
- Gehring, H
- Jansonius, J N
- Christen, P
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Citations
Graber, R., Kasper, P., Malashkevich, V. N., Strop, P., Gehring, H., Jansonius, J. N., & Christen, P. (1999). Conversion of aspartate aminotransferase into an L-aspartate beta-decarboxylase by a triple active-site mutation. Journal of Biological Chemistry, 274(44), 31203–31325. https://doi.org/10.1074/jbc.274.44.31203
