Ascaris suum: cloning of a cDNA encoding phosphoenolpyruvate carboxykinase.
A cDNA encoding phosphoenolpyruvate carboxykinase (PEPCK) from Ascaris suum was cloned by complementation of a strain of Escherichia coli deficient in PEPCK and malic enzyme. The product of this cDNA was enzymatically similar to a recombinant PEPCK obtained from Haemonchus contortus by the same method. Comparison of the predicted amino acid sequence of A. suum PEPCK with other PEPCKs showed that this enzyme is most closely related to the H. contortus enzyme. The two nematode enzymes share considerable homology in regions thought to be functionally involved in substrate binding and catalysis, some of which distinguish the nematode enzymes from PEPCKs from other organisms. This analysis suggests a structural explanation for the kinetic differences seen between nematode and vertebrate PEPCKs and supports the hypothesis that nematode PEPCK is a target for selective inhibition.
Upjohn Laboratories, Upjohn Company, Kalamazoo, Michigan 49001.
T G
TG
Geary
C A
CA
Winterrowd
S J
SJ
Alexander-Bowman
M A
MA
Favreau
S C
SC
Nulf
R D
RD
Klein
D000595:Amino Acid Sequence; D000818:Animals; D017165:Ascaris suum / Q000201:enzymology* / Q000235:genetics; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics*; D006189:Haemonchus / Q000201:enzymology; D008969:Molecular Sequence Data; D010729:Phosphoenolpyruvate Carboxykinase (GTP) / Q000235:genetics*; D017386:Sequence Homology, Amino Acid
D004247:DNA; D010729:Phosphoenolpyruvate Carboxykinase (GTP)