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- W2091234760 abstract "Abstract The maximal velocity, V, for isocitrate cleavage by isocitrate lysase from Pseudomonas indigofera was dependent on two dissociable groups (pKa's of 6.9 and 8.6). The pH dependence of the pKi for succinate, a product of isocitrate cleavage, implied that a dissociable group (pKa of 6.0) on the enzyme functions in binding succinate. The pKi's for maleate and itaconate (succinate analogs) were similarly pH dependent. The pKi for oxalate, an analog of glyoxylate which is also a product of isocitrate cleavage, was pH independent. In contrast the pKi's of the four-carbon dicarboxylic acid inhibitors, fumarate and meso-tartrate, both of which affect the glyoxylate site, were dependent on a dissociable group on the enzyme-inhibitor complex. Comparison of the pH dependence of the pKm for isocitrate and the pKi for succinate (and succinate analogs) indicated that the binding of isocitrate was dependent on an acidic dissociable group on the enzyme (pKa of 5.8). The pH dependence of the pKi for homoisocitrate was similar. In addition the Ki for succinate and Km for isocitrate were dependent upon Mg2+ concentration. Inhibition by phosphoenolpyruvate, which binds to the succinate site and may regulate isocitrate lyase from P. indigofera, was twice as pH dependent as that for succinate. Two dissociable groups, one on the enzyme (pKa of 5.8) and one on phosphoenolpyruvate (pKa of 6.35), contributed to the pH dependence observed with phosphoenolpyruvate." @default.
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- W2091234760 date "1976-06-01" @default.
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- W2091234760 title "Isocitrate lyase from Pseudomonas indigofera: pH dependence of catalysis and binding of substrates and inhibitors" @default.
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- W2091234760 doi "https://doi.org/10.1016/0003-9861(76)90400-8" @default.
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