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Gene Review

folA  -  dihydrofolate reductase

Escherichia coli UTI89

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Disease relevance of folA


High impact information on folA


Chemical compound and disease context of folA


Biological context of folA


Anatomical context of folA


Associations of folA with chemical compounds

  • Calculations for wild-type dihydrofolate reductase and a triple mutant, along with the associated single and double mutants, indicate that each enzyme system samples a unique distribution of coupled motions correlated to hydride transfer [24].
  • Mammalian expression modules encoding the dominant marker neomycin phosphotransferase or the amplifiable dihydrofolate reductase gene expressed from SV40 promoters were inserted for use in gene transfer studies [25].
  • DHFR was modified to permit the covalent addition of a fluorescent molecule, Alexa 488, and a biotin at the N terminus of the molecule [18].
  • Three of the strains produced dihydrofolate reductase with an increased Ki value for trimethoprim [26].
  • In the formation of the ternary complex with NADPH, trimethoprim bound to dihydrofolate reductase as if all the enzyme existed as a single species with a KD for trimethoprim of 1.9 nM [14].

Physical interactions of folA


Other interactions of folA


Analytical, diagnostic and therapeutic context of folA


  1. Mapping and sequencing of the dihydrofolate reductase gene (DFR1) of Saccharomyces cerevisiae. Barclay, B.J., Huang, T., Nagel, M.G., Misener, V.L., Game, J.C., Wahl, G.M. Gene (1988) [Pubmed]
  2. Cloning of the Escherichia coli K-12 dihydrofolate reductase gene following mu-mediated transposition. Rood, J.I., Laird, A.J., Williams, J.W. Gene (1980) [Pubmed]
  3. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate. Bolin, J.T., Filman, D.J., Matthews, D.A., Hamlin, R.C., Kraut, J. J. Biol. Chem. (1982) [Pubmed]
  4. Species-specific irreversible inhibition of Neisseria gonorrhoeae dihydrofolate reductase by a substituted 2,4-diamino-5-benzylpyrimidine. Tansik, R.L., Averett, D.R., Roth, B., Paterson, S.J., Stone, D., Baccanari, D.P. J. Biol. Chem. (1984) [Pubmed]
  5. The structure of the mutant dihydrofolate reductase from Streptococcus faecium. Amino acid sequence of peptide CNBr 7 and complete sequence of the protein. Peterson, D.L., Gleisner, J.M., Blakley, R.L. J. Biol. Chem. (1975) [Pubmed]
  6. Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria. Eilers, M., Schatz, G. Nature (1986) [Pubmed]
  7. Functional role of aspartic acid-27 in dihydrofolate reductase revealed by mutagenesis. Howell, E.E., Villafranca, J.E., Warren, M.S., Oatley, S.J., Kraut, J. Science (1986) [Pubmed]
  8. The SecA and SecY subunits of translocase are the nearest neighbors of a translocating preprotein, shielding it from phospholipids. Joly, J.C., Wickner, W. EMBO J. (1993) [Pubmed]
  9. Neutron diffraction studies of Escherichia coli dihydrofolate reductase complexed with methotrexate. Bennett, B., Langan, P., Coates, L., Mustyakimov, M., Schoenborn, B., Howell, E.E., Dealwis, C. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  10. Use of the Escherichia coli chromosomal DHFR gene as selection marker in mammalian cells. Asselbergs, F.A., Widmer, R. J. Biotechnol. (1995) [Pubmed]
  11. CsgD, a regulator of curli and cellulose synthesis, also regulates serine hydroxymethyltransferase synthesis in Escherichia coli K-12. Chirwa, N.T., Herrington, M.B. Microbiology (Reading, Engl.) (2003) [Pubmed]
  12. Switching tRNA(Gln) identity from glutamine to tryptophan. Rogers, M.J., Adachi, T., Inokuchi, H., Söll, D. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  13. Role of aspartate 27 of dihydrofolate reductase from Escherichia coli in interconversion of active and inactive enzyme conformers and binding of NADPH. Appleman, J.R., Howell, E.E., Kraut, J., Blakley, R.L. J. Biol. Chem. (1990) [Pubmed]
  14. Interconvertible forms of Escherichia coli dihydrofolate reductase with different affinities for analogs of dihydrofolate. Pattishall, K.H., Burchall, J.J., Harvey, R.J. J. Biol. Chem. (1976) [Pubmed]
  15. Cloning and nucleotide sequence of a negative regulator gene for Klebsiella aerogenes arylsulfatase synthesis and identification of the gene as folA. Azakami, H., Sugino, H., Murooka, Y. J. Bacteriol. (1992) [Pubmed]
  16. Directed mutagenesis of dihydrofolate reductase. Villafranca, J.E., Howell, E.E., Voet, D.H., Strobel, M.S., Ogden, R.C., Abelson, J.N., Kraut, J. Science (1983) [Pubmed]
  17. Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis. McElheny, D., Schnell, J.R., Lansing, J.C., Dyson, H.J., Wright, P.E. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  18. Interaction of dihydrofolate reductase with methotrexate: ensemble and single-molecule kinetics. Rajagopalan, P.T., Zhang, Z., McCourt, L., Dwyer, M., Benkovic, S.J., Hammes, G.G. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  19. Antifolate-resistant Chinese hamster cells. Molecular basis for the biochemical and structural heterogeneity among dihydrofolate reductases produced by drug-sensitive and drug-resistant cell lines. Melera, P.W., Davide, J.P., Oen, H. J. Biol. Chem. (1988) [Pubmed]
  20. Ricin A chain can transport unfolded dihydrofolate reductase into the cytosol. Beaumelle, B., Taupiac, M.P., Lord, J.M., Roberts, L.M. J. Biol. Chem. (1997) [Pubmed]
  21. Substrate requirements of hepatitis C virus serine proteinase for intermolecular polypeptide cleavage in Escherichia coli. Komoda, Y., Hijikata, M., Sato, S., Asabe, S., Kimura, K., Shimotohno, K. J. Virol. (1994) [Pubmed]
  22. Development of a chaperone-deficient system by fractionation of a prokaryotic coupled transcription/translation system. Kudlicki, W., Mouat, M., Walterscheid, J.P., Kramer, G., Hardesty, B. Anal. Biochem. (1994) [Pubmed]
  23. Refolding of recombinant Pneumocystis carinii dihydrofolate reductase and characterization of the enzyme. Delves, C.J., Ballantine, S.P., Tansik, R.L., Baccanari, D.P., Stammers, D.K. Protein Expr. Purif. (1993) [Pubmed]
  24. Impact of distal mutations on the network of coupled motions correlated to hydride transfer in dihydrofolate reductase. Wong, K.F., Selzer, T., Benkovic, S.J., Hammes-Schiffer, S. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  25. Cosmid vectors for rapid genomic walking, restriction mapping, and gene transfer. Wahl, G.M., Lewis, K.A., Ruiz, J.C., Rothenberg, B., Zhao, J., Evans, G.A. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  26. Amplification and modification of dihydrofolate reductase in Escherichia coli. Nucleotide sequence of fol genes from mutationally altered plasmids. Smith, D.R., Rood, J.I., Bird, P.I., Sneddon, M.K., Calvo, J.M., Morrison, J.F. J. Biol. Chem. (1982) [Pubmed]
  27. The cloning and DNA sequence of the gene for the glutathione-regulated potassium-efflux system KefC of Escherichia coli. Munro, A.W., Ritchie, G.Y., Lamb, A.J., Douglas, R.M., Booth, I.R. Mol. Microbiol. (1991) [Pubmed]
  28. Inhibition of thymidylate synthetase and dihydrofolate reductase by naturally occurring oligoglutamate derivatives of folic acid. Friedkin, M., Plante, L.T., Crawford, E.J., Crumm, M. J. Biol. Chem. (1975) [Pubmed]
  29. An essential intermediate in the folding of dihydrofolate reductase. Heidary, D.K., O'Neill, J.C., Roy, M., Jennings, P.A. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  30. Effect of N-bromosuccinimide modification on dihydrofolate reductase from a methotrexate-resistant strain of Escherichia coli. Activity, spectrophotometric, fluorescence and circular dichroism studies. Williams, M.N. J. Biol. Chem. (1975) [Pubmed]
  31. Deletion analysis of a multifunctional yeast tRNA ligase polypeptide. Identification of essential and dispensable functional domains. Apostol, B.L., Westaway, S.K., Abelson, J., Greer, C.L. J. Biol. Chem. (1991) [Pubmed]
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