Chalcone dimethylallyltransferase from Morus nigra cell cultures. Substrate specificity studies.

Andrea Silvestrini, Alberto Vitali, Bruno Giardina, Andrea Tafi, Bruno Botta

Risultato della ricerca: Contributo in rivistaArticolo in rivistapeer review

21 Citazioni (Scopus)

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 Mg(2+), to be effective. The apparent K(m) values for gamma,gamma-dimethylallyldiphosphate and 2',4'-dihydroxychalcone were 63 and 142 microM, respectively. The maximum activity of the enzyme was expressed during the first 10 days of cell growth.
Lingua originaleEnglish
pagine (da-a)33-38
Numero di pagine6
RivistaFEBS Letters
Stato di pubblicazionePubblicato - 2004

Keywords

  • prenyltransferase

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