| Literature DB >> 5661493 |
Abstract
This paper describes some new characteristics of the phosphoenolpyruvate carboxykinase CO(2)-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 CO(2)-oxaloacetate exchange reaction in higher plants and animals.Entities:
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Year: 1968 PMID: 5661493 PMCID: PMC1086925 DOI: 10.1104/pp.43.5.788
Source DB: PubMed Journal: Plant Physiol ISSN: 0032-0889 Impact factor: 8.340