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Chalcone dimethylallyltransferase from Morus nigra cell cultures. Substrate specificity studies

2003; Wiley; Volume: 557; Issue: 1-3 Linguagem: Inglês

10.1016/s0014-5793(03)01398-x

1873-3468

Alberto Vitali, Bruno Giardina, Giuliano Delle Monache, Filippo Della Rocca, Andrea Silvestrini, Andrea Tafi, Bruno Botta,

Plant Gene Expression Analysis

A new prenyltransferase (PT) enzyme derived from the microsomal fractions of cell cultures of Morus nigra was shown to be able to prenylate exclusively chalcones with a 2′,4′‐dihydroxy substitution and the isoflavone genistein. Computational studies were performed to shed some light on the relationship between the structure of the substrate and the enzymatic activity. PT requires divalent cations, particularly Mg 2+ , to be effective. The apparent K m values for γ,γ‐dimethylallyldiphosphate and 2′,4′‐dihydroxychalcone were 63 and 142 μM, respectively. The maximum activity of the enzyme was expressed during the first 10 days of cell growth.