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

FEBS Letters

Seidler, Andreas²  Beyer, Peter³  Neuhaus, Gunther³  Schledz, Michael¹ 

[1] Greenovation Pflanzenbiotechnologie GmBH, Bötzinger Str. 29b, D-79111 Freiburg, Germany;Fakultät für Biologie/Biochemie der Pflanzen, Ruhr-Universität Bochum, D-44780 Bochum, Germany;Center for Applied Biosciences, University of Freiburg, Schänzlestr. 1, D-79104 Freiburg, Germany

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;   

DOI  :  10.1016/S0014-5793(01)02508-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown