Characterization of Key Glycolytic and Oxidative Enzymes in Steinernema carpocapsae


  • J. J. M. Shih
  • E. G. Platzer
  • S. N. Thompson
  • E. J. Carroll, Jr.


The enzyme activities of isocitrate dehydrogenase (ICDH, NADP-specific), lactate dehydrogenase (LDH), malate dehydrogenase (MDH), phosphoenolpyruvate carboxykinase (PEPCK), phosphofructokinase (PFK), pyruvate kinase (PK), and fructose-l,6-bisphosphatase (FBPase) were studied in the third-stage juveniles of Steinernema carpocapsae. Reaction requirements, pH optima, substrate and cofactor kinetic constants were similar to those reported previously from other parasitic helminths with the exception of LDH, which was unstable and could not be characterized for specific activity and kinetic constants. The respective pH optima were 7.5 for ICDH, 8.8 for MDH, 6.5 for PEPCK, 7.3 for PFK, 7.2 for PK, and 7.5 for FBPase. The specific activities for ICDH, MDH, PEPCK, PFK, PK, and FBPase at pH 7.5 were 4.8, 1,300, 22, 25, 35, and 6.8 (nmoles substrate · min[sup-]¹ · mg protein[sup-]¹), respectively. In summary, the infective juveniles of S. carpocapsae display the metabolism typical of a facultative aerobe. Key words: aerobic metabolism, anaerobic metabolism, biochemistry, carbon dioxide fixation, entomopathogenic nematode, enzyme, facuhative anaerobiosis, gluconeogenesis, glycolysis, intermediary metabolism, nematode, Steinernema carpocapsae.