Publication: Conversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature
Conversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature
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Mouratou, B., Kasper, P., Gehring, H., & Christen, P. (1999). Conversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature. Journal of Biological Chemistry, 274, 1320–1325. https://doi.org/10.1074/jbc.274.3.1320
Abstract
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Abstract
Tyrosine phenol-lyase (TPL), which catalyzes the beta-elimination reaction of L-tyrosine, and aspartate aminotransferase (AspAT), which catalyzes the reversible transfer of an amino group from dicarboxylic amino acids to oxo acids, both belong to the alpha-family of vitamin B6-dependent enzymes. To switch the substrate specificity of TPL from L-tyrosine to dicarboxylic amino acids, two amino acid residues of AspAT, thought to be important for the recognition of dicarboxylic substrates, were grafted into the active site of TPL. Homolog
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- Mouratou, B
- Kasper, P
- Gehring, H
- Christen, P
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Mouratou, B., Kasper, P., Gehring, H., & Christen, P. (1999). Conversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature. Journal of Biological Chemistry, 274, 1320–1325. https://doi.org/10.1074/jbc.274.3.1320
