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• W2115343224 startingPage "764" @default.
• W2115343224 abstract "The repressive effects of exogenous cytidine on growing cells was examined in a specially constructed strain in which the pool sizes of endogenous uridine 5'-diphosphate and uridine 5'-triphosphate cannot be varied by the addition of uracil and/or uridine to the medium. Five enzymes of the pyrimidine biosynthetic pathway and one enzyme of the arginine biosynthetic pathway were assayed from cells grown under a variety of conditions. Cytidine repressed the synthesis of dihydroorotase (encoded by pyrC), dihydroorotate dehydrogenase (encoded by pyrD), and ornithine transcarbamylase (encoded by argI). Moreover, aspartate transcarbamylase (encoded by pyrB) became further derepressed upon cytidine addition, whereas no change occurred in the levels of the last two enzymes (encoded by pyrE and pyrF) of the pyrimidine pathway. Quantitative nucleotide pool determinations have provided evidence that any individual ribo- or deoxyribonucleoside mono-, di-, or triphosphate of cytosine or uracil is not a repressing metabolite for the pyrimidine biosynthetic enzymes. Other nucleotide derivatives or ratios must be considered." @default.
• W2115343224 created "2016-06-24" @default.
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• W2115343224 date "1975-11-01" @default.
• W2115343224 modified "2023-10-02" @default.
• W2115343224 title "Pyrimidine biosynthetic enzymes of Salmonella typhimurium, repressed specifically by growth in the presence of cytidine" @default.
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• W2115343224 doi "https://doi.org/10.1128/jb.124.2.764-774.1975" @default.
• W2115343224 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/235966" @default.
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