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[Alpha-hydroxy-acid dehydrogenase activity in Trypanosoma cruzi]
Acta Physiologica Latino Americana
|January 1, 1976
Summary
Trypanosoma cruzi epimastigotes catalyze alpha-ketoacid to alpha-hydroxyacid conversion, regenerating nicotinamide adenine dinucleotide (NAD). This suggests a role in anaerobic energy metabolism and flagellar activity.
Area of Science:
- Biochemistry
- Parasitology
- Enzymology
Context:
- Investigates metabolic pathways in Trypanosoma cruzi culture forms.
- Focuses on epimastigote stage enzymatic activity.
- Explores substrate utilization and enzyme kinetics.
Purpose:
- To characterize the alpha-hydroxyacid dehydrogenase activity in Trypanosoma cruzi.
- To determine the enzyme's substrate specificity and kinetic properties.
- To elucidate the potential role of this enzyme in parasite metabolism.
Summary:
- Crude extracts from Trypanosoma cruzi epimastigotes exhibit alpha-hydroxyacid dehydrogenase activity, converting various alpha-ketoacids to their corresponding alpha-hydroxyacids.
- The enzyme demonstrates Michaelian kinetics for some substrates (alpha-ketocaproate, alpha-ketoisocaproate, alpha-ketoglutarate) but bimodal kinetics for others.
- Electrophoretic analysis indicates a single protein is responsible for the observed enzymatic activity across different substrates.
- This activity allows for pyruvate to lactate interconversion and nicotinamide adenine dinucleotide (NAD) regeneration in anaerobic conditions.
Impact:
- Demonstrates Trypanosoma cruzi's capacity for NAD regeneration, crucial for anaerobic survival.
- Highlights potential similarities between Trypanosoma cruzi's metabolic pathways and those in mammalian/avian spermatozoa.
- Suggests a possible link between this enzymatic activity and flagellar function in the parasite.