tailieunhanh - Báo cáo khoa học: A novel mechanism of V-type zinc inhibition of glutamate dehydrogenase results from disruption of subunit interactions necessary for efficient catalysis

Bovine glutamate dehydrogenase is potently inhibited by zinc and the major impact is on Vmaxsuggesting a V-type effect on catalysis or product release. Zinc inhibition decreases as glutamate concentrations decrease suggesting a role for subunit interactions. | IFEBS Journal A novel mechanism of V-type zinc inhibition of glutamate dehydrogenase results from disruption of subunit interactions necessary for efficient catalysis Jaclyn Bailey1 Lakeila Powell2 Leander Sinanan3 Jacob Neal3 Ming Li4 Thomas Smith4 and Ellis Bell3 1 Gustavus Adolphus College St Peter MN USA 2 Virginia State University Petersburg VA USA 3 Department of Chemistry University of Richmond VA USA 4 Donald Danforth Plant Science Center St Louis MO USA Keywords allostery glutamate dehydrogenase protein dynamics subunit interactions zinc inhibition Correspondence E. Bell Department of Chemistry University of Richmond Richmond VA 23173 USA Fax 1 804 287 1897 Tel 1 804 289 8244 E-mail jbell2@ Received 9 March 2011 revised 13 June 2011 accepted 7 July 2011 doi Bovine glutamate dehydrogenase is potently inhibited by zinc and the major impact is on Vmax suggesting a V-type effect on catalysis or product release. Zinc inhibition decreases as glutamate concentrations decrease suggesting a role for subunit interactions. With the monocarboxylic amino acid norvaline which gives no evidence of subunit interactions zinc does not inhibit. Zinc significantly decreases the size of the pre-steady state burst in the reaction but does not affect NADPH binding in the enzyme-NADPH-gluta-mate complex that governs the steady state turnover again suggesting that zinc disrupts subunit interactions required for catalytic competence. While differential scanning calorimetry suggests zinc binds and induces a slightly conformationally more rigid state of the protein limited proteolysis indicates that regions in the vicinity of the antennae regions and the trimer-tri-mer interface become more flexible. The structures of glutamate dehydrogenase bound with zinc and europium show that zinc binds between the three dimers of subunits in the hexamer a region shown to bind novel inhibitors that block catalytic turnover which is consistent with the

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