A novel phytyltransferase from Synechocystis sp. PCC 6803 involved in tocopherol biosynthesis
Open Access
- 14 June 2001
- journal article
- Published by Wiley in FEBS Letters
- Vol. 499 (1-2) , 15-20
- https://doi.org/10.1016/s0014-5793(01)02508-x
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.Keywords
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