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- W257543934 abstract "The discovery of deoxycytidylate deaminase resulted from independent investigations on the metabolism of deoxycytidine derivatives in sea urchin eggs and in rat embryo extracts. At the time, the deaminase appeared to provide the only direct means of forming deoxyuridine monophosphate (dUMP), a substrate for the critical enzyme thymidylate synthetase, and it was viewed as playing a possible role in the regulation of DNA synthesis or contributing to the efficiency of pyrimidine nucleotide utilization. Potential evidence in support of these assumptions was provided by studies indicating that deaminase activity was elevated in mitotically active normal and neoplastic tissues. The role of the deaminase in most bacterial systems is marginal at best or non-existent, except in those cases where the enzyme is induced on bacteriophage infection, and even in this case, the presence of the enzyme is not essential for survival. In the course of studies, the enzyme to be markedly susceptible to feedback inhibition by deoxycytidine triphosphate (dCTP) and deoxythymidine triphosphate (dTTP) has been found, and it has proved to be a convenient model for the study of the mechanisms involved in eliciting allosteric transitions associated with deoxycytidylate deaminase." @default.
- W257543934 created "2016-06-24" @default.
- W257543934 creator A5006391092 @default.
- W257543934 creator A5068505847 @default.
- W257543934 date "1972-01-01" @default.
- W257543934 modified "2023-09-26" @default.
- W257543934 title "The Regulatory Influence of Allosteric Effectors on Deoxycytidylate Deaminases" @default.
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- W257543934 doi "https://doi.org/10.1016/b978-0-12-152805-8.50012-5" @default.
- W257543934 hasPublicationYear "1972" @default.
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