TY - JOUR T1 - CYP98A6 from Lithospermum erythrorhizon encodes 4-coumaroyl-4'-hydroxyphenyllactic acid 3-hydroxylase involved in rosmarinic acid biosynthesis JF - FEBS Lett Y1 - 2002 A1 - Michiyo Matsuno A1 - Akito Nagatsu A1 - Yukio Ogihara A1 - Brian E Ellis A1 - Hajime Mizukami SP - 219–24 KW - Acetates KW - Cell Extracts KW - Cells: Cultured KW - Cinnamates KW - Cloning: Molecular KW - Cyclopentanes KW - Cytochrome P-450 Enzyme System KW - Depsides KW - DNA: Complementary KW - Gene Expression KW - Gene Expression Profiling KW - Lithospermum KW - Mixed Function Oxygenases KW - Molecular Sequence Data KW - Oxylipins KW - Phenylalanine Ammonia-Lyase KW - Phenylpropionates KW - Phylogeny KW - Plant Proteins KW - RNA: Messenger AB - Rosmarinic acid is the dominant hydroxycinnamic acid ester accumulated in Boraginaceae and Lamiaceae plants. A cytochrome P450 cDNA was isolated by differential display from cultured cells of Lithospermum erythrorhizon, and the gene product was designated CYP98A6 based on the deduced amino acid sequence. After expression in yeast, the P450 was shown to catalyze the 3-hydroxylation of 4-coumaroyl-4'-hydroxyphenyllactic acid, one of the final two steps leading to rosmarinic acid. The expression level of CYP98A6 is dramatically increased by addition of yeast extract or methyl jasmonate to L. erythrorhizon cells, and its expression pattern reflected the elicitor-induced change in rosmarinic acid production, indicating that CYP98A6 plays an important role in regulation of rosmarinic acid biosynthesis. VL - 514 ER -