4.5 Article

Characterization of homogentisate prenyltransferases involved in plastoquinone-9 and tocochromanol biosynthesis

Journal

FEBS LETTERS
Volume 580, Issue 22, Pages 5357-5362

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2006.09.002

Keywords

plastoquinone-9; tocopherol; prenyltransferases; homogentisate; 2-methyl-6-solanesyl-1,4-benzoquinol; substrate specificity

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A cDNA of Chlamydomonas reinhardtii encoding a plastidial homogentisate prenyltransferase was identified. Functional expression studies in Escherichia coli revealed that the enzyme possessed properties similar to the prenyltransferase of Arabidopsis thaliana encoded by At3g11950 but different from the phytyltransferases of A. thaliana and Synechocystis. Unlike the phytyltransferases, the C reinhardtii and the respective A. thaliana enzyme showed highest activities with solanesyl diphosphate, but were hardly active with phytyl diphosphate. Hence, these data pro-tide evidence that the latter represent homogentisate solanesyltransferases; involved in plastoquinone-9 biosynthesis. Overexpression of At3g11950 in A. thaliana, however, suggests that the solanesyltransferase can affect tocopherol biosynthesis as well. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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