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Methylation of 4-thio-2′-deoxyuridylate by thymidylate synthetase

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
55
Issue
1
Identifiers
DOI: 10.1016/s0006-291x(73)80081-6
Disciplines
  • Biology

Abstract

Summary 4-Thio-2′-deoxyuridylate was found to be a substrate for the thymidylate synthetase of a dichloromethotrexate resistant strain of Lactobacillus casei. The enzymic product which contained the carbon derived from formaldehyde, was identified as 4-thiothymidylate by chromatographic analysis. 4-Thio-2′-deoxyuridylate inhibited the methylation of deoxyuridylate with an apparent K i of 7×10 −5 M, reflecting its lower affinity for the enzyme as compared to the natural substrate. 4-Thio-2′-deoxyuridylate is, so far, the only substrate analog modified in the base which is methylated by thymidylate synthetase.

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