The Protein Journal

, Volume 30, Issue 8, pp 546–548 | Cite as

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. AllemannEmail author


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.


Dihydrofolate reductase Moritella profunda Trimethoprim Inhibition 



Dihydrofolate reductase


Dihydrofolate reductase from Moritella profunda


Dihydrofolate reductase from Escherichia coli


Circular dichroism


Sodium dodecyl sulfate polyacrylamide gel electrophoresis



Funding for this work was provided by the UK. Engineering and Physical Sciences Research Council (Doctoral Training Grant to R.M.E.), the Leonardo da Vinci Programme (A.S.) and Cardiff University.


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Copyright information

© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  • E. Joel Loveridge
    • 1
  • William M. Dawson
    • 1
  • Rhiannon M. Evans
    • 1
    • 2
  • Anna Sobolewska
    • 1
    • 3
  • Rudolf K. Allemann
    • 1
    Email author
  1. 1.School of ChemistryCardiff UniversityCardiffUK
  2. 2.Inorganic Chemistry LaboratoryUniversity of OxfordOxfordUK
  3. 3.Manchester Interdisciplinary Biocentre, Faculty of Life SciencesUniversity of ManchesterManchesterUK

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