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Chalcone dimethylallyltransferase from Morus nigra cell cultures. Substrate specificity studies
Author(s) -
Vitali Alberto,
Giardina Bruno,
Delle Monache Giuliano,
Rocca Filippo,
Silvestrini Andrea,
Tafi Andrea,
Botta Bruno
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01398-x
Subject(s) - prenyltransferase , chalcone , enzyme , substrate (aquarium) , divalent , chemistry , biochemistry , enzyme assay , stereochemistry , biology , prenylation , organic chemistry , ecology
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.