Dihydrofolate reductases from chicken liver and Lactobacillus casei bind Cibacron blue F3GA in different modes and at different sites.

Dihydrofolate reductase: partial sequence of the Lactobacillus casei enzyme and homology with other dihydrofolate reductases [proceedings].

Species-specific irreversible inhibition of Neisseria gonorrhoeae dihydrofolate reductase by a substituted 2,4-diamino-5-benzylpyrimidine.

Neisseria gonorrhoeae dihydrofolate reductase undergoes a time-dependent, irreversible inactivation by 2,4-diamino-5-[3,5-dimethoxy-4-(p-bromoacetamidophenoxy)benzyl] pyrimidine. The kinetics of inactivation are consistent with the reversible formation of an enzyme-inhibitor complex followed by covalent binding to the enzyme. The reversible component is competitive with dihydrofolate and has an...

Characterization of the DNA binding region recognized by dihydrofolate reductase from lactobacillus casei.

Two specific DNA binding sites for the enzyme dihydrofolate reductase from Lactobacillus casei have been located by means of an immunoprecipitation assay within a 2900-base pair L. casei DNA fragment containing the L. casei dihydrofolate reductase structural gene, which was previously cloned into pBR322. The inserted L. casei DNA was mapped using restriction endonucleases, and the location and ...

DNA binding by dihydrofolate reductase from Lactobacillus casei.

The protein-dependent retention of double-stranded DNA molecules on nitrocellulose filters has been used to show that pure dihydrofolate reductase from Lactobacillus casei has affinity for DNA. Dihydrofolate reductase will bind to end-labeled linear double-stranded DNA and to DNA in supercoiled form. Coenzymes and certain inhibitors do not affect the affinity of the protein to DNA, indicating t...

Structure and dynamics in solution of the complex of Lactobacillus casei dihydrofolate reductase with the new lipophilic antifolate drug trimetrexate.

We have determined the three-dimensional solution structure of the complex of Lactobacillus casei dihydrofolate reductase and the anticancer drug trimetrexate. Two thousand seventy distance, 345 dihedral angle, and 144 hydrogen bond restraints were obtained from analysis of multidimensional NMR spectra recorded for complexes containing 15N-labeled protein. Simulated annealing calculations produ...