Abstract
AbstractThe effect of the carbon source succinate on pyrimidine synthesis in the pathogen Burkholderia cepacia ATCC 25416 was investigated. The five de novo pathway enzyme activities of pyrimidine biosynthesis in B. cepacia were shown to be affected when ATCC 25416 cells were grown in the presence of uracil. Pyrimidine limitation of a uracil auxotrophic B. cepacia strain lacking orotidine 5′‐monophosphate decarboxylase activity increased aspartate transcarbamoylase, dihydroorotase, dihydroorotate dehydrogenase and orotate phosphoribosyltransferase activities by at least 1.5‐fold which indicated that these pathway enzymes may be regulated by a uracil‐related compound. The levels of the de novo pyrimidine biosynthetic enzyme activities in B. cepacia ATCC 25416 cells appeared to be influenced to a greater degree in cells grown on succinate than on glucose as a carbon source.
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