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

Protein J. 2011 Dec;30(8):546-8. doi: 10.1007/s10930-011-9361-x.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Folic Acid Antagonists / pharmacology*
  • Glutamic Acid / chemistry
  • Glutamic Acid / genetics*
  • Glutamic Acid / metabolism
  • Kinetics
  • Moritella / chemistry
  • Moritella / enzymology*
  • Moritella / genetics
  • Mutation, Missense*
  • Tetrahydrofolate Dehydrogenase / chemistry*
  • Tetrahydrofolate Dehydrogenase / genetics
  • Tetrahydrofolate Dehydrogenase / metabolism
  • Trimethoprim / pharmacology*

Substances

  • Bacterial Proteins
  • Folic Acid Antagonists
  • Glutamic Acid
  • Trimethoprim
  • Tetrahydrofolate Dehydrogenase