The free-living planarianPolycelis nigra has a complete sequence of glycolytic and tricarboxylic acid cycle enzymes together with an active betaoxidation sequence. Neither octopine dehydrogenase nor any other of the pyruvate: amino acid-linked dehydrogenases was present inP. nigra. The lactate dehydrogenase of this planarian was, however, unusual in being activated by fructose-1,6-bisphosphate.
The steady state contents of the glycolytic and tricarboxylic acid cycle intermediates were measured in quick frozenP. nigra. A comparison of the mass action ratios with the equilibrium constants for the glycolytic reactions showed that phosphoglucomutase, glucosephosphate isomerase, aldolase, triosephosphate isomerase, phosphoglyceromutase and phosphopyruvate hydratase reactions are all near equilibrium, whilst phosphofructokinase and pyruvate kinase reactions are displaced from equilibrium. No phosphagen or phosphagen phosphotransferase activity could be detected inP. nigra but it is possible that the high levels of 3-phosphoglycerate could function as an alternative store of high energy phosphate.
Under anaerobic conditionsP. nigra produces lactic acid; there is no evidence for the production of succinate, acetate or propionate, acids characteristically produced by parasitic platyhelminths.
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Barrett, J., Butterworth, P.E. Carbohydrate and lipid catabolism in the planarianPolycelis nigra . J Comp Physiol B 146, 107–112 (1982). https://doi.org/10.1007/BF00688723
- Pyruvate Kinase
- Tricarboxylic Acid Cycle
- Triosephosphate Isomerase