Analysis of the metal requirement of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli
作者： C.M. Stephens , R. Bauerle
DOI: 10.1016/S0021-9258(18)54781-5
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摘要: The three isozymes of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli were overproduced, purified, and characterized with respect to their requirement for metal cofactor. isolated contained 0.2-0.3 mol iron/mol enzyme monomer, variable amounts zinc, traces copper. Enzymatic activity the native enzymes was stimulated 3-4-fold by addition Fe2+ ions reaction mixture eliminated treatment EDTA. chelated reactivated a variety divalent ions, including Ca2+, Cd2+, Co2+, Cu2+, Fe2+, Mn2+, Ni2+, Zn2+. specific activities varied widely different metals as follows: Mn2+ greater than Co2+ Zn2+ much Ca2+. Steady state kinetic analysis forms phenylalanine-sensitive isozyme (DAHPS(Phe)) revealed that variation significantly affected apparent affinity substrate, erythrose 4-phosphate, but not second phosphoenolpyruvate, or feedback inhibitor, L-phenylalanine. tetrameric DAHPS(Phe) exhibited positive homotropic cooperativity phophoenolpyruvate, phenylalanine in presence all tested.
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