2′-Deoxy-2′-fluorouridine-5′-phosphate: an alternative substrate for thymidylate synthetase from Escherichia coli K12

The substrate specificity of 2′-deoxy-2′-substituted uridines and their 5′-phosphates towards thymidylate synthetase from Escherichia coli K12 was investigated. Besides the natural substrate 2′-deoxyuridine-5′-phosphate (dUMP), only 2′-deoxy-2′-fluorouridine-5′-phosphate (dUfIMP) was a substrate. Th...

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Bibliographic Details
Published in:Nucleic acids research 1978-12, Vol.5 (12), p.4753-4760
Main Authors: Wohlrab, Franz, Haertlé, Tomasz, Trichtinger, Thomas, Guschlbauer, Wilhelm
Format: Article
Language:English
Subjects:
Deoxyuracil Nucleotides
Escherichia coli
Escherichia coli - enzymology
Fluorodeoxyuridylate
Kinetics
Methyltransferases - metabolism
Molecular Conformation
Substrate Specificity
Thymidylate Synthase - metabolism
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Summary:The substrate specificity of 2′-deoxy-2′-substituted uridines and their 5′-phosphates towards thymidylate synthetase from Escherichia coli K12 was investigated. Besides the natural substrate 2′-deoxyuridine-5′-phosphate (dUMP), only 2′-deoxy-2′-fluorouridine-5′-phosphate (dUfIMP) was a substrate. The KM of dUfIMP is 11 times higher than that of dUMP, while the Vmax values are virtually the same. It is concluded that the size of the 2′-substituent and not its polarity (and the concomitant conformational change) determines substrate specificity of thymidylate synthetase.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/5.12.4753