Deoxycytidine Triphosphate Deaminase: Identification and Function in Salmonella typhimurium

J. Neuhard, E. Thomassen
1971 Journal of Bacteriology  
The biosynthesis of 2'-deoxyuridine monophosphate (dUMP) has been studied in a cytidineL and uracil-requiring mutant of Salmonella typhimurium (DP-55). The dUMP pool and the thymidine monophosphate (dTMP) pool of DP-55, grown in the presence of 3H-uracil and unlabeled cytidine, are found to have the same specific activities. However, only 30% of the dUMP and the dTMP is synthesized from a uridine nucleotide. Seventy per cent is derived directly from a cytosine compound. The identification and
more » ... rtial purification of a Mg2+-dependent 2'-deoxycytidine triphosphate (dCTP) deaminase from S. typhimurium suggests that the combined action of dCTP deaminase and 2'-deoxyuridine triphosphate pyrophosphatase accounts for 70% of the dUMP, and therefore the dTMP, synthesized in vivo. The introduction of a thymine requirement (i.e., a block in thymidylate synthetase) into DP-55 results in a 100-fold increase in the size of the dUMP pool. However, the relative contribution of the uridine and cytidine pathways to dUMP synthesis is unaltered. The high dUMP pool is accompanied by extensive catabolism of dUMP to uracil. Partial thymine starvation of the cells results in a significant increase in the dUMP and dCTP pools. Moreover, an increase in the contribution of the dCTP pathway to dUMP synthesis is observed. As a result of these changes the catabolism of dUMP to uracil is augmented. Bacterial mutants defective in cytidine triphosphate (CTP) synthetase (pyrG) require cytidine on May 9, 2020 by guest
doi:10.1128/jb.105.2.657-665.1971 fatcat:v6hxudir6napbiqpnb7vddo5h4