Stage-specific expression of aldolase isoenzymes in the rodent malaria parasite Plasmodium berghei.
We have cloned two gene (aldo-1 and aldo-2) encoding the glycolytic enzyme aldolase of the rodent malaria parasite Plasmodium berghei. The amino acid sequence of one gene product, ALDO-1, is virtually identical to P. falciparum aldolase whereas ALDO-2, the second gene product, is different and has 13% sequence diversity to ALDO-1. We expressed ALDO-2 as an active enzyme in Escherichia coli and compared the biochemical and kinetic properties to that of P. falciparum recombinant aldolase (ALDO-1 type). Based on the Km and Vmax constants for FMP and FBP, neither ALDO-1 nor ALDO-2 can be clearly assigned to any of the known mammalian isoenzyme classes. We demonstrate that expression of the two isoenzymes is developmentally regulated: specific antibody probes detect ALDO-1 in sporozoite stages of P. berghei and ALDO-2 is found in blood stage parasites.
Meier
B
B
Department of PRT, F. Hoffmann-La Roche, Ltd., Basel, Switzerland.
Döbeli
H
H
Certa
U
U
D000595:Amino Acid Sequence; D000818:Animals; D005075:Biological Evolution; D015153:Blotting, Western; D003001:Cloning, Molecular; D005634:Fructose-Bisphosphate Aldolase / Q000096:biosynthesis* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D007527:Isoenzymes / Q000096:biosynthesis* / Q000235:genetics / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D010962:Plasmodium berghei / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D015183:Restriction Mapping; D016415:Sequence Alignment; D013379:Substrate Specificity
D007527:Isoenzymes; D005634:Fructose-Bisphosphate Aldolase