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. 1972 Jun;49(6):893–897. doi: 10.1104/pp.49.6.893

Purification and Properties of Adenosine Diphosphoglucose Pyrophosphorylase from Sweet Corn 1

Jacob Amir a,2, Joe H Cherry a
PMCID: PMC366074  PMID: 16658078

Abstract

A 40-fold purification of adenosine diphosphoglucose pyrophosphorylase from sweet corn (Zea mays var. Golden Beauty) revealed the enzyme to be specific for adenosine triphosphate. The enzyme has an absolute requirement for Mg2+ and is activated by 3-phosphoglycerate and to a lesser extent by ribose-5-phosphate and fructose-6-phosphate. The apparent Km values of the enzyme for glucose-1-phosphate, adenosine triphosphate, pyrophosphate, and adenosine diphosphoglucose are 1.9 × 10−4, 3.2 × 10−5, 3.3 × 10−5, and 6.2 × 10−4m, respectively. Pyrophosphate inhibits adenosine diphosphoglucose synthesis competitively (Ki = 3.8 × 10−7m), while orthophosphate and sulfate appear to inhibit the reacion noncompetitively. These results show that the production of this sugar nucleotide can be controlled by the concentration of pyrophosphate.

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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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