Journal of Comparative Physiology B

, Volume 164, Issue 3, pp 247–255 | Cite as

Enzyme activity profiles in an overwintering population of freeze-tolerant larvae of the gall fly, Eurosta solidaginis

  • D. R. Joanisse
  • K. B. Storey


The activity of some enzymes of intermediary metabolism, including enzymes of glycolysis, the hexose monophosphate shunt, and polyol cryoprotectant synthesis, were measured in freeze-tolerant Eurosta solidaginis larvae over a winter season and upon entry into pupation. Flexible metabolic rearrangement was observed concurrently with acclimatization and development. Profiles of enzyme activities related to the metabolism of the cryoprotectant glycerol indicated that fall biosynthesis may occur from two possible pathways: 1. glyceraldehyde-phosphate → glyceraldehyde → glycerol, using glyceraldehyde phosphatase and NADPH-linked polyol dehydrogenase, or 2. dihydroxyacetonephosphate → glycerol-3-phosphate → glycerol, using glycerol-3-phosphate dehydrogenase and glycerol-3-phosphatase. Clearance of glycerol in the spring appeared to occur by a novel route through the action of polyol dehydrogenase and glyceraldehyde kinase. Profiles of enzyme activities associated with sorbitol metabolism suggested that this polyol cryoprotectant was synthesized from glucose-6-phosphate through the action of glucose-6-phosphatase and NADPH-linked polyol dehydrogenase. Removal of sorbitol in the spring appeared to occur through the action of sorbitol dehydrogenase and hexokinase. Glycogen phosphorylase activation ensured the required flow of carbon into the synthesis of both glycerol and sorbitol. Little change was seen in the activity of glycolytic or hexose monophosphate shunt enzymes over the winter. Increased activity of the α-glycerophosphate shuttle in the spring, indicated by greatly increased glycerol-3-phosphate dehydrogenase activity, may be key to removal and oxidation of reducing equivalents generated from polyol cryoprotectan catabolism.

Key words

Insect freeze tolerance Enzymes Metabolism Cryoprotectant synthesis Eurosta solidaginis 



6-Phosphogluconate dehydrogenase


dihydroxy acetone phosphate










glycerol-3-phosphate phophatase


glycerol-3-phosphate dehydrogenase






glucose-6-phosphate dehydrogenase


glyceraldehyde kinase






glyceraldehyde-3-phosphate dehydrogenase


glycerol dehydrogenase


glycogen phosphorylase


hexose monophosphate shunt


lactate dehydrogenase


NADP+-dependent isocitrate dehydrogenase


polyol dehydrogenase, glyceraldehyde activity


polyol dehydrogenase, glucose activity






phosphoglycerate kinase




pyruvate kinase




sorbitol dehydrogenase


maximal enzyme activity


wet weight


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Copyright information

© Springer-Verlag 1994

Authors and Affiliations

  • D. R. Joanisse
    • 1
    • 2
  • K. B. Storey
    • 1
    • 2
  1. 1.Institute of BiochemistryCarleton UniversityOttawaCanada
  2. 2.Department of BiologyCarleton UniversityOttawaCanada

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