Phosphoenolpyruvate Carboxylation and Aspartate Synthesis in Acetobacter suboxydans1
AUTOR(ES)
Claus, G. W.
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=249747Documentos Relacionados
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