Glyoxylate pathway in the free-living stages of the entomophilic nematode Romanomermis culicivorax
Journal of Nematology
Isocitrate lyase and malate synthetase, key enzymes of the glyoxylate cycle, were present in postparasites of R. culicivorax. Specific activities of enzymes were higher in adult postparasites than in newly emerged juveniles. Isocitrate lyase had a well-defined pH optimum (7.5), whereas malate synthetase functioned optimally over a broad range of alkaline pH (7.5-9.0). Substrate affinities of the 2 enzymes were measured..