Chalcone dimethylallyltransferase from Morus nigra cell cultures. Substrate specificity studies

FEBS Letters

Giardina, Bruno³  Delle Monache, Giuliano³  Tafi, Andrea¹  Silvestrini, Andrea³  Botta, Bruno²  Rocca, Filippo³  Vitali, Alberto³ 

[1]Dipartimento Farmaco Chimico Tecnologico, Università di Siena, Piazza Aldo Moro, 44100 Siena, Italy

[2]Dipartimento di Studi di Chimica e Tecnologia delle Sostanze Biologicamente Attive, Università ‘La Sapienza’, P.le A. Moro 5, 00185 Rome, Italy

[3]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

关键词: Prenyltransferase;    γ;    γ-Dimethylallyldiphosphate;    Product specificity;    Molecular modeling;    PT;    prenyltransferase;    2;    4-D;    2;    4-dihydrochlorophenoxyacetic acid;    DTT;    dithiothreitol;    DMAPP;    dimethylallylpyrophosphate;   

DOI  :  10.1016/S0014-5793(03)01398-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 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.

【 授权许可】

Unknown