Abstract:
:Prenylation reactions contribute considerably to the diversity of natural products. Polyprenylated secondary metabolites include hyperforin which is both quantitatively and pharmacologically a major constituent of the medicinal plant Hypericum perforatum (St. John's wort). Cell cultures of the related species Hypericum calycinum were found to contain a prenyltransferase activity which is likely to catalyze the first prenylation step in hyperforin biosynthesis. The enzyme was soluble and dependent on a divalent cation, with Fe2+ leading to maximum activity (Km=3.8 mM). The preferred prenyl donor was DMAPP (Km=0.46 mM) and the preferred prenyl acceptor was phlorisobutyrophenone (Km=0.52 mM). A broad pH optimum from 6.5 to 8.5 and a temperature optimum from 35 to 40 degrees C were observed. The formation of hyperforins in H. calycinum cell cultures was preceded by an increase in dimethylallyltransferase activity, with the maximum specific activity being 3.6 microkat/kg protein.
journal_name
Phytochemistryjournal_title
Phytochemistryauthors
Boubakir Z,Beuerle T,Liu B,Beerhues Ldoi
10.1016/j.phytochem.2004.10.020subject
Has Abstractpub_date
2005-01-01 00:00:00pages
51-7issue
1eissn
0031-9422issn
1873-3700pii
S0031-9422(04)00553-9journal_volume
66pub_type
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