Abstract
The enzymatic formation of m-geranyl- p-hydroxybenzoic acid from geranylpyrophosphate and p-hydroxybenzoic acid was investigated in cell-free extracts of Lithospermum erythrorhizon cell cultures. The reaction required the presence of a divalent cation, magnesium being the most effective activator. The enzyme showed a very broad pH optimum between pH 7.1 and 9.3. It was highly specific for both p-hydroxybenzoic acid and geranylpyrophosphate, and the apparent K m values for these two substrates were 0.014 and 0.56 mM, respectively. The activity was located in the pellet of a 100 000 g centrifugation, showing that the enzyme is bound to membranes or microsomes. Shikonin-producing cultures contained an activity of this enzyme 35 times higher than non-producing cultures, suggesting that this enzyme is of regulatory importance in shikonin biosynthesis.
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