Properties and inhibition of thymidylate synthetase in Drosophila melanogaster.

@article{Carpenter1974PropertiesAI,
  title={Properties and inhibition of thymidylate synthetase in Drosophila melanogaster.},
  author={Nancy J. Carpenter},
  journal={Journal of insect physiology},
  year={1974},
  volume={20 7},
  pages={
          1389-401
        }
}
A quantitative comparison of the incorporation of methyl-sHthymidine and 6-sH-deoxyuridine into the DNA of Drosophila nzelanogaster in the presence and in the absence of 5-fluorouracil indicated that S-fluorouracil inhibits the reaction converting dUMP to dTMP catalysed by thymidylate synthetase (methylenetetrahydrofolate:dUrd-5’-P C-methyltransferase, E.C. 2.1.1 .b). The enzyme exhibits maximal activity at pH 7.5 to 8-O and is protected from heat inactivation by deoxyuridine monophosphate. The… CONTINUE READING
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