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.
Vitali, A., Giardina, B., Delle Monache, G., Rocca, F., Silvestrini, A., Tafi, A., Botta, B., Chalcone dimethylallyltransferase from Morus nigra cell cultures. Substrate specificity studies., <<FEBS LETTERS>>, 2004; (557): 33-38. [doi:10.1016/S0014-5793(03)01398-X] [http://hdl.handle.net/10807/21242]
Chalcone dimethylallyltransferase from Morus nigra cell cultures. Substrate specificity studies.
Vitali, Alberto;Giardina, Bruno;Silvestrini, Andrea;
2004
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.
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
