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• W1526354648 abstract "Crude extracts of Mycobacterium smegmatis catalyzed the synthesis of adenosine diphosphate-glucose (ADP-Glc), cytidine diphosphate-glucose, guanosine diphosphate-glucose (GDP-Glc), thymidine diphosphate-glucose (TDP-Glc), and uridine diphosphate-glucose (UDP-Glc). In these crude enzyme fractions, high concentrations of trehalose-P inhibited the ADP-Glc and GDP-Glc pyrophosphorylases but did not effect the UDP-Glc or TDP-Glc pyrophosphorylases. Both the ADP-Glc pyrophosphorylase and the UDP-Glc pyrophosphorylase were partially purified (about 140-fold and 60-fold, respectively), and their properties were compared. For the ADP-Glc pyrophosphorylase, the K m for adenosine triphosphate was 6 × 10 −4 m , whereas that for glucose-1-P was 8 × 10 −4 m . The optimal concentration of Mg 2+ was 1 × 10 −3 m , and the p H optimum was 8.5. For the UDP-Glc pyrophosphorylase, the K m for uridine triphosphate was 1 × 10 −3 m and for glucose-1-P was 2 × 10 −3 m . The optimal Mg 2+ concentration was 1 × 10 −3 m , and the p H optimum was about 8.0. The purified ADP-Glc pyrophosphorylase was inhibited by fructose-6-P, fructose-1, 6-diphosphate, glucose-6-P, and phosphoenolpyruvate. On the other hand, trehalose, trehalose diphosphate, sodium pyruvate, and ribose-5-P did not effect the ADP-Glc pyrophosphorylase. None of these compounds, including trehalose-P, had any effect on the UDP-Glc pyrophosphorylase." @default.
• W1526354648 created "2016-06-24" @default.
• W1526354648 creator A5052467439 @default.
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• W1526354648 date "1972-10-01" @default.
• W1526354648 modified "2023-10-18" @default.
• W1526354648 title "Purification and Properties of the Adenosine Diphosphate-Glucose and Uridine Diphosphate-Glucose Pyrophosphorylases of <i>Mycobacterium smegmatis</i> : Inhibition and Activation of the Adenosine Diphosphate-Glucose Pyrophosphorylase" @default.
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• W1526354648 doi "https://doi.org/10.1128/jb.112.1.327-336.1972" @default.
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