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. 1976 Dec;58(6):753–756. doi: 10.1104/pp.58.6.753

Regulatory Properties of the ADP-Glucose Pyrophosphorylase of the Blue-Green Bacterium Synechococcus 6301 1

Carolyn Levi a, Jack Preiss a
PMCID: PMC542302  PMID: 16659760

Abstract

ADP-glucose was found to be the primary sugar nucleotide used for glycogen synthesis by Synechococcus 6301. ADP-glucose pyrophosphorylase was partially purified 12-fold from this blue-green bacterium. The enzyme was activated 8- to 25-fold by glycerate 3-phosphate. Fructose 6-phosphate, fructose 1,6-bisphosphate, 5′-adenylate, and adenosine diphosphate activated the enzyme, but less than glycerate 3-phosphate. The enzyme was inhibited by inorganic phosphate. The I0.5 of phosphate was 0.072 mm, and in the presence of 2 mm glycerate 3-phosphate, increased to 1.8 mm. The substrate saturation curves for glucose 1-phosphate and ATP were hyperbolic in both the presence and absence of glycerate 3-phosphate or phosphate. The saturation curve for MgCl2 was sigmoidal; 2 mm glycerate 3-phosphate decreased the sigmoidicity from a Hill slope n value of 5.6 to 2.8, and increased the MgCl2 optimum from 3 mm to 6 to 7 mm.

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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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