Abstract
This paper describes some new characteristics of the phosphoenolpyruvate carboxykinase CO2-oxaloacetate exchange reaction in purified preparations of Rhodospirillum rubrum. The enzymatic activity has been purified 169-fold. Nucleotide diphosphates substitute for nucleotide triphosphates in the exchange reaction. Nucleotide diphosphates will not support the synthesis of phosphoenolpyruvate from oxaloacetate. This reaction differs significantly from the CO2-oxaloacetate exchange reaction in higher plants and animals.
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Selected References
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