Hydroxymethyldihydropterin pyrophosphokinase from Plasmodium falciparum complements a folK-knockout mutant in E. coli when expressed as a separate polypeptide detached from dihydropteroate synthase.
Jönsson
Maria
M
Department of Medical Biochemistry and Microbiology, Uppsala University Biomedical Centre, Box 582, SE-75123 Uppsala, Sweden. Maria.Jonsson@imbim.uu.se
Swedberg
Göte
G
D000818:Animals; D004094:Dihydropteroate Synthase / Q000378:metabolism*; D017854:Diphosphotransferases / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D017353:Gene Deletion; D015870:Gene Expression; D009097:Multienzyme Complexes / Q000235:genetics; D010963:Plasmodium falciparum / Q000201:enzymology* / Q000235:genetics; D013762:Tetrahydrofolate Dehydrogenase / Q000235:genetics; D013940:Thymidylate Synthase / Q000235:genetics
D009097:Multienzyme Complexes; C056930:thymidylate synthase-dihydrofolate reductase; D013762:Tetrahydrofolate Dehydrogenase; D013940:Thymidylate Synthase; D004094:Dihydropteroate Synthase; D017854:Diphosphotransferases; C019684:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase