Stage-specific expression of aldolase isoenzymes in the rodent malaria parasite Plasmodium berghei

Mol Biochem Parasitol. 1992 May;52(1):15-27. doi: 10.1016/0166-6851(92)90032-f.


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.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biological Evolution
  • Blotting, Western
  • Cloning, Molecular
  • Fructose-Bisphosphate Aldolase / biosynthesis*
  • Fructose-Bisphosphate Aldolase / genetics
  • Fructose-Bisphosphate Aldolase / metabolism
  • Humans
  • Isoenzymes / biosynthesis*
  • Isoenzymes / genetics
  • Isoenzymes / metabolism
  • Kinetics
  • Molecular Sequence Data
  • Plasmodium berghei / enzymology*
  • Plasmodium berghei / genetics
  • Plasmodium berghei / growth & development
  • Restriction Mapping
  • Sequence Alignment
  • Substrate Specificity


  • Isoenzymes
  • Fructose-Bisphosphate Aldolase

Associated data

  • GENBANK/M81793