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. 1969 Feb;97(2):691–696. doi: 10.1128/jb.97.2.691-696.1969

Phosphoenolpyruvate Carboxylation and Aspartate Synthesis in Acetobacter suboxydans1

G W Claus a, M L Orcutt a, R T Belly a
PMCID: PMC249747  PMID: 5773023

Abstract

Dialyzed extracts of Acetobacter suboxydans ATCC 621 catalyze 14CO2 assimilation in the presence of phosphoenolpyruvate and a divalent cation. The formation of 14C-oxalacetate was demonstrated and found not to be dependent upon the presence of orthophosphate or diphosphonucleotides. Oxalacetate synthesis was stimulated by orthophosphate and inhibited by aspartate. All attempts to demonstrate a reversible carboxylation mechanism have failed. 14C-aspartate was synthesized when phosphoenolpyruvate, H14Co3−, pyridoxal phosphate, and glutamate were added to dialyzed extracts. Chromatographic and spectrophotometric analyses and chemical degradation further demonstrate the presence of a reversible aspartate aminotransferase. The function of oxalacetate synthesis in a bacterium that reportedly lacks an operative tricarboxylic acid cycle is discussed.

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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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