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Lett Appl Microbiol. 1995 Nov;21(5):340-3.

Pyrimidine synthesis in Burkholderia cepacia ATCC 25416.

Author information

1
Olson Biochemistry Laboratories, Department of Chemistry and Biochemistry, South Dakota State University, Brookings, USA.

Abstract

Pyrimidine synthesis in the food spoilage agent Burkholderia cepacia ATCC 25416 was investigated. The five de novo pathway enzymes of pyrimidine biosynthesis were found to be active in B. cepacia ATCC 25416 and growth of this strain on uracil had an effect on the de novo enzyme activities. The in vitro regulation of aspartate transcarbamoylase activity in B. cepacia ATCC 25416 was studies and its activity was inhibited by PP(i), ATP, GTP, CTP and UTP. The enzymes cytidine deaminase, uridine phosphorylase and cytosine deaminase were found to be active in the salvage of pyrimidines in ATCC 25416. Overall, de novo pyrimidine synthesis in B. cepacia ATCC 25416 was regulated at the level of enzyme activity and its pyrimidine salvage enzymes differed from those found in B. cepacia ATCC 17759.

PMID:
7576530
[Indexed for MEDLINE]

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