Reduced susceptibility of moritella profunda dihydrofolate reductase to trimethoprim is not due to glutamate 28

E. Joel Loveridge, William M. Dawson, Rhiannon M. Evans, Anna Sobolewska, Rudolf K. Allemann*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

1 Citation (Scopus)

Abstract

The E28D variant of dihydrofolate reductase from Moritella profunda was generated and found to have the same K i (within error) for the competitive inhibitor trimethoprim as the wild type enzyme. Contrary to a previous claim in the literature, Glu 28 is therefore not the cause of the reduced affinity for trimethoprim relative to dihydrofolate reductase from Escherichia coli.

Original languageEnglish
Pages (from-to)546-548
Number of pages3
JournalProtein Journal
Volume30
Issue number8
DOIs
Publication statusPublished - 1 Dec 2011

Keywords

  • Dihydrofolate reductase
  • Inhibition
  • Moritella profunda
  • Trimethoprim

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