Abstract
The development of bacterial strains which lack the enzymes for the interconversion of cytidine and uridine has allowed the identity of the putative effectors of the pyrimidine pathway to be more firmly established. In Salmonella typhimurium it has previously been show that the formation of carbamyl phosphate synthetase, encoded by the gene pyrA, is controlled by a cytidine nucleotide and arginine. The synthesis of aspartate transcarbamylase, encoded pyrB, is primarily controlled by a uridine compound. In further studies (encoded by pyrD), orotidine-5'-monophosphate (OMP) pyrophosphorylase (encoded by pyrE) and OMP decarboxylase (encoded by pyrF), were examined and found to be primarily affected by a cytidine compound. In this study, using a specially constructed strain of Enterobacter aerogenes, which lacked dihydroorotase (encoded by pyrC) and cytidine deaminase (encoded by cdd), it was found that aspartate transcarbamylase was affected to the greatest extent by a uridine compound. ...
Deutsch, Walter Andrew (1974). Control of pyrimidine biosynthesis and metabolism of pyrimidine nucleosides and nucleotides in Enterobacter aerogenes. Doctoral dissertation, Texas A&M University. Texas A&M University. Libraries. Available electronically from
https : / /hdl .handle .net /1969 .1 /DISSERTATIONS -170240.