title: Reduced susceptibility of Moritella profunda dihydrofolate reductase to trimethoprim is not due to glutamate 28.
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.
authors.affiliation: School of Chemistry, Cardiff University, Park Place, Cardiff, UK.
authors.forename: E Joel
authors.initials: EJ
authors.lastname: Loveridge
authors.forename: William M
authors.initials: WM
authors.lastname: Dawson
authors.forename: Rhiannon M
authors.initials: RM
authors.lastname: Evans
authors.forename: Anna
authors.initials: A
authors.lastname: Sobolewska
authors.forename: Rudolf K
authors.initials: RK
authors.lastname: Allemann
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D005493:Folic Acid Antagonists / Q000494:pharmacology*; D018698:Glutamic Acid / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D007700:Kinetics; D034221:Moritella / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics; D020125:Mutation, Missense; D013762:Tetrahydrofolate Dehydrogenase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D014295:Trimethoprim / Q000494:pharmacology*
chemical_list: D001426:Bacterial Proteins; D005493:Folic Acid Antagonists; D018698:Glutamic Acid; D014295:Trimethoprim; D013762:Tetrahydrofolate Dehydrogenase