Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4886
Title: Chalcone Prenyltransferase from Morus nigra cell cultures. Substrate specificity studies
Authors: Vitali, A.
Botta, B.
Tafi, Andrea 
Silvestrini, A.
DELLE MONACHE, G.
Giardina, B.
Rocca, F.
Issue Date: 2004
Project: None 
Journal: FEBS LETTERS
Abstract: 
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 Mg2+, to be effective. The apparent K-m values for gamma,gamma-dimethylallyldiphosphate and 2',4'-dihydroxychalcone were 63 and 142 muM, respectively. The maximum activity of the enzyme was expressed during the first 10 days of cell growth.
Description: 
19386
URI: http://hdl.handle.net/20.500.12779/4886
ISSN: 0014-5793
DOI: 10.1016/S0014-5793(03)01398-X
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