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• W2328951844 abstract "MenD catalyzes the thiamin diphosphate-dependent decarboxylative carboligation of α-ketoglutarate and isochorismate. The enzyme is essential for menaquinone biosynthesis in many bacteria and has been proposed to be an antibiotic target. The kinetic mechanism of this enzyme has not previously been demonstrated because of the limitations of the UV-based kinetic assay. We have reported the synthesis of an isochorismate analogue that acts as a substrate for MenD. The apparent weaker binding of this analogue is advantageous in that it allows accurate kinetic experiments at substrate concentrations near Km. Using this substrate in concert with the dead-end inhibitor methyl succinylphosphonate, an analogue of α-ketoglutarate, we show that MenD follows a ping-pong kinetic mechanism. Using both the natural and synthetic substrates, we have measured the effects of 12 mutations of residues at the active site. The results give experimental support to previous models and hypotheses and allow observations unavailable using only the natural substrate." @default.
• W2328951844 created "2016-06-24" @default.
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• W2328951844 date "2011-09-19" @default.
• W2328951844 modified "2023-09-27" @default.
• W2328951844 title "Using Substrate Analogues To Probe the Kinetic Mechanism and Active Site of <i>Escherichia coli</i> MenD" @default.
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• W2328951844 doi "https://doi.org/10.1021/bi201202n" @default.
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