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- W2000860134 abstract "The maximal velocity, V, for isocitrate cleavage by isocitrate lyase from Neurospora crassa is dependent on two dissociable groups with pKa values of 6.1 and 8.6. A dissociable group with a pKa of 8.5 on the enzyme-substrate complex affects the pKm for isocitrate. The pKi for homoisocitrate is affected in a like manner. The pH dependence of the pKi's for succinate, a product of isocitrate cleavage, and the succinate analog maleate is similar to the pH dependence of the pKm of isocitrate below pH 7.3, but is markedly different above this pH. Both the Km for isocitrate and the Ki for succinate were dependent upon Mg2+ concentration. The pKi for oxalate, an analog of glyoxylate which is also a product of isocitrate cleavage, is dependent on a group with a pKa of 6.8 on the enzyme-inhibitor complex. The pH dependence of the pKi for phosphoenolpyruvate, which binds to the succinate site, suggests that it is dependent on two dissociable groups, one on phosphoenolpyruvate and one, by analogy to the pKm for isocitrate, on the enzyme-glyoxylate-inhibitor complex." @default.
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- W2000860134 date "1977-04-01" @default.
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- W2000860134 title "Isocitrate lyase from Neurospora crassa: pH Dependence of catalysis and interaction with substrates and inhibitors" @default.
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- W2000860134 doi "https://doi.org/10.1016/0003-9861(77)90048-0" @default.
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