A novel phytyltransferase from Synechocystis sp. PCC 6803 involved in tocopherol biosynthesis

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• 作者：Schledz ; Michael ; Seidler ; Andreas ; Beyer ; Peter ; Neuhaus ; Gunther
• 关键词：Prenyl/phytyltransferase ; Plastoquinone ; Vitamin E ; Tocopherol ; Synechocystis ; ORF ; open reading frame ; TLC ; thin layer chromatography ; PP ; diphosphate ; E_m ; molar extinction coefficient
• 刊名：FEBS Letters
• 出版年：2001
• 出版时间：June 15, 2001
• 年：2001
• 卷：499
• 期：1-2
• 页码：15-20
• 全文大小：373 K

文摘

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.