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- W2065399285 abstract "—The hydrolysis of ThTP by rat brain membrane-bound ThTPase is inhibited by nucleoside diphosphates and triphosphates. ATP and ADP are most effective, reducing hydrolysis by 50% at concentrations of 2 × 10−5m and 7·5 × 10−5m respectively. Nucleoside monophosphates and free nuclcosides as well as Pi have no effect on enzyme activity. ThMP and ThDP also fail to inhibit hydrolysis in concentrations up to 5 × 10−3m. Non-hydrolysable methylene phosphate analogs of ATP and ADP were used in further kinetic studies with the ThTPase. The mechanism of inhibition by these analogs is shown to be of mixed non-competitive nature for both compounds. An observed Ki, of 4 × 10−5m for the ATP analog adenosine-PPCP and 9 × 10−5m for the ADP analog adenosine-PCP is calculated at pH 6·5. Formation of the true enzyme substrate, the [Mg2+. ThTP] complex, is not significantly affected by concentrations of analogs producing maximal (>95%) inhibition of enzyme activity. Likewise the relationships between pH and observed Km and pH and Vmax are not shifted by the presence of similar concentrations of inhibitor." @default.
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- W2065399285 date "2006-10-04" @default.
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- W2065399285 title "MEMBRANE THIAMINE TRTPHOSPHATASE FROM RAT BRAIN: INHIBITION BY ATP AND ADP" @default.
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- W2065399285 doi "https://doi.org/10.1111/j.1471-4159.1976.tb04441.x-i1" @default.
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