Data di Pubblicazione:
1999
Citazione:
Inhibitor binding studies on ascorbate oxidase / L. Casella, E. Monzani, L. Santagostini, L. Gioia, M. Gullotti, P. Fantucci, T. Beringhelli, A. Marchesini. - In: COORDINATION CHEMISTRY REVIEWS. - ISSN 0010-8545. - 185-6(1999), pp. 619-628.
Abstract:
The characteristic features of the plant multicopper enzyme ascorbate
oxidase are described, together with the current knowledge about its
catalytic mechanism and substrate specificity. A variety of small
anionic inhibitors have been used as spectroscopic probes for the enzyme
metal sites, but recently interest has arisen for a new type of phenolic
inhibitors which act competitively against ascorbate. These simple
phenolic compounds can bind to the enzyme in the same pocket near type 1
copper as the substrate ascorbate binds, as shown by docking and
molecular mechanics computations. (C) 1999 Elsevier Science S.A. All
rights reserved.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
Ascorbate oxidase; Catalytic mechanism; Enzyme inhibition; Molecular mechanics; Spectroscopic studies
Elenco autori:
L. Casella, E. Monzani, L. Santagostini, L. Gioia, M. Gullotti, P. Fantucci, T. Beringhelli, A. Marchesini
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