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J. Biol. Chem., Vol. 277, Issue 8, 6240-6246, February 22, 2002
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From the Molecular & Cellular Biology of Totipotency, Division of
Integrated Life Science, Graduate School of Biostudies, Kyoto
University, Kitashirakawa, Kyoto 606-8502, Japan
Two cDNAs encoding geranyl
diphosphate:4-hy- droxybenzoate 3-geranyltransferase were isolated from
Lithospermum erythrorhizon by nested PCR using the
conserved amino acid sequences among polyprenyl- transferases for
ubiquinone biosynthesis. They were functionally expressed in yeast
COQ2 disruptant and showed a strict substrate specificity
for geranyl diphosphate as the prenyl donor, in contrast to ubiquinone
biosynthetic enzymes, suggesting that they are involved in the
biosynthesis of shikonin, a naphthoquinone secondary metabolite. Regulation of their expression by various culture conditions coincided with that of geranyltransferase activity and the secondary metabolites biosynthesized via this enzyme. This is the first established plant
prenyltransferase that transfers the prenyl chain to an aromatic substrate.
Geranyl Diphosphate:4-Hydroxybenzoate Geranyltransferase from
Lithospermum erythrorhizon
CLONING AND CHARACTERIZATION OF A KEY ENZYME IN SHIKONIN
BIOSYNTHESIS*
,
*
This work was supported in part by a grant-in-aid for
Scientific Research from the Japanese Society for Promotion of Science (to K. Y.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Molecular & Cellular Biology of Totipotency, Div. of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Kitashirakawa, Kyoto
606-8502, Japan. Tel.: 81-75-753-6384; Fax: 81-75-753-6398; E-mail:
yazaki@ kais.kyoto-u.ac.jp.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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