A novel phytyltransferase from Synechocystis sp. PCC 6803 involved in tocopherol biosynthesis. |
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Authors: | M Schledz A Seidler P Beyer G Neuhaus |
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Affiliation: | Greenovation Pflanzenbiotechnologie GmBH, Freiburg, Germany. mschledz@greenovation.com |
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Abstract: | The deduced polypeptide sequence of open reading frame slr1736 reveals homology to chlorophyll synthase and 1,4-dihydroxy-2-naphthoic acid phytyltransferase in Synechocystis sp. strain PCC 6803. In tocopherol and plastoquinone biosynthesis, a condensation reaction mechanistically similar to that of these two enzymes is performed. To analyze the function of this novel prenyltransferase, a deletion mutant of slr1736 was generated by homologous recombination. The mutant showed a markedly decreased tocopherol content, while plastoquinone levels remained unchanged. Since the aromatic precursor homogentisic acid accumulated in the mutant, the function of the enzyme was proven to be a novel tocopherol phytyltransferase. |
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