A bifunctional thymidylate synthetase-dihydrofolate reductase in protozoa.
Thymidylate synthetase and dihydrofolate reductase exist as a bifunctional protein in a number of species of protozoa which span diverse groups of the subkingdom. The enzymes copurify upon gel filtration and on affinity chromatography columns specific for dihydrofolate reductase. The bifunctional protein has been found in species of Crithidia, Leishmania, Trypanosoma, Plasmodium, Eimeria, Tetrahymena and Euglena. For reasons unknown, neither enzyme could be detected in Entamoeba histolytica or E. invadens. Since neither enzyme has yet been found as a separate protein in protozoa, it is likely that the bifunctional protein is widespread among these primitive eukaryotes. In most cases, the apparent size of the native protein is approximately twice that of the subunit possessing thymidylate synthetase. Further, with one exception, the subunit sizes are close to the sum of the subunit sizes of the separate enzymes found in other sources.
D000818:Animals; D056890:Eukaryota / Q000201:enzymology*; D008780:Methyltransferases / Q000302:isolation & purification*; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000302:isolation & purification*; D013762:Tetrahydrofolate Dehydrogenase / Q000302:isolation & purification*; D013940:Thymidylate Synthase / Q000302:isolation & purification*
D009097:Multienzyme Complexes; D013762:Tetrahydrofolate Dehydrogenase; D008780:Methyltransferases; D013940:Thymidylate Synthase