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Pyrimidine Metabolism in Streptomyces griseus

Salvage of pyrimidine nucleosides and bases by S. griseus and the regulation of aspartate transcarbamoylase (ATCase) were studied. The velocity-substrate curve for S. griseus ATCase was hyperbolic for both aspartate and carbamoylphosphate. The enzyme activity was diminished in the presence of ATP, CTP, or UTP. The synthesis of ATCase was repressed in cells grown in the presence of exogenous uracil. The specific activity of cells grown with uracil was 43 percent of that for cells grown in minimal medium only. Maximal ATCase and dihydroorotase activities were found in the same column fraction after size-exclusion chromatography, suggesting that both activities could reside in the same polypeptide. The pyrimidine salvage enzymes cytosine deaminase and uridine phosphorylase were identified in S. griseus using HPLC reversed-phase chromatography.

Identiferoai:union.ndltd.org:unt.edu/info:ark/67531/metadc278710
Date08 1900
CreatorsHughes, Lee E. (Lee Everette)
ContributorsO'Donovan, Gerard A., Benjamin, Robert C., Shanley, Mark Stephen
PublisherUniversity of North Texas
Source SetsUniversity of North Texas
LanguageEnglish
Detected LanguageEnglish
TypeThesis or Dissertation
FormatText
RightsPublic, Copyright, Copyright is held by the author, unless otherwise noted. All rights reserved., Hughes, Lee E. (Lee Everette)

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