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Crude extracts ofMycobacterium 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, theK m for adenosine triphosphate was 6 × 10−4 m , whereas that for glucose-1-P was 8 × 10−4 m . The optimal concentration of Mg2+ was 1 × 10−3 m , and thep H optimum was 8.5. For the UDP-Glc pyrophosphorylase, theK m for uridine triphosphate was 1 × 10−3 m and for glucose-1-P was 2 × 10−3 m . The optimal Mg2+ concentration was 1 × 10−3 m , and thep 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.

journal of bacteriology

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

Purification and Properties of the Adenosine Diphosphate-Glucose and Uridine Diphosphate-Glucose Pyrophosphorylases of Mycobacterium smegmatis : Inhibition and Activation of the Adenosine Diphosphate-Glucose Pyrophosphorylase