[Comparative topography of the catalytic sites of chromosomal dihydrofolate reductases and that of the enzyme encoded in R 67 plasmid from E. coli].
The trimethoprim-resistant dihydrofolate reductase specified in E. coli by plasmid R 67, when compared, with other enzymes catalyzing the same reaction, to have a dissimilar primary, secondary, tertiary and quaternary structure. In regard to the tertiary structure, we show here that the pteridine binding site, in the plasmid-encoded enzyme, has a geometrical similarity with that of other chromosomal specified reductases.
D001665:Binding Sites; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D008958:Models, Molecular; D010957:Plasmids; D013762:Tetrahydrofolate Dehydrogenase / Q000235:genetics / Q000378:metabolism*; D014295:Trimethoprim / Q000494:pharmacology
D014295:Trimethoprim; D013762:Tetrahydrofolate Dehydrogenase
Topographie comparée des sites catalytiques des dihydrofolates réductases d'origine chromosomique et de l'enzyme codé par le plasmide R 67 de E. coli.