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BIBTEX RIS

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

1978; Oxford University Press; Volume: 5; Issue: 12 Linguagem: Inglês

10.1093/nar/5.12.4753

ISSN

1362-4962

Autores

Franz Wohlrab, Thomas Haertlé, Thomas Trichtinger, Wilhelm Guschlbauer,

Tópico(s)

Enzyme Structure and Function

Resumo

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 (dUflMP) was a substrate. The KM of dUflMP 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.

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