Chalcone dimethylallyltransferase from Morus nigra cell cultures. Substrate specificity studies.
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
Alberto
A
Istituto di Chimica del Riconoscimento Molecolare, Sezione di Roma, Istituto di Biochimica e Biochimica Clinica, Università Cattolica del S. Cuore, Largo F. Vito 1, 00168 Rome, Italy. a.vitali@uniserve.ccr.rm.cnr.it
Giardina
Bruno
B
Delle Monache
Giuliano
G
Rocca
Filippo
F
Silvestrini
Andrea
A
Tafi
Andrea
A
Botta
Bruno
B
D002478:Cells, Cultured; D002599:Chalcone / Q000031:analogs & derivatives / Q000737:chemistry* / Q000378:metabolism*; D004122:Dimethylallyltranstransferase / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D008861:Microsomes / Q000201:enzymology; D008968:Molecular Conformation; D031625:Morus / Q000201:enzymology*; D013379:Substrate Specificity
D002599:Chalcone; D004122:Dimethylallyltranstransferase