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. 1972 Oct;112(1):327–336. doi: 10.1128/jb.112.1.327-336.1972

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

David Lapp a,1, Alan D Elbein a
PMCID: PMC251415  PMID: 5079067

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

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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