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[Temperature causes structural and functional changes in lactate dehydrogenase from fish skeletal muscles]
Biofizika
|July 1, 1993
Summary
Fish muscle adaptation to temperature alters lactate dehydrogenase (LDH) enzyme properties. Cold-adapted fish LDH is more stable and kinetically different from warm-adapted fish LDH, with urea treatment reversing these changes.
Area of Science:
- Biochemistry
- Enzymology
- Comparative Physiology
Context:
- Organisms adapt to environmental temperatures through physiological and biochemical changes.
- Lactate dehydrogenase (LDH) is a key enzyme in cellular respiration, crucial for energy production in fish skeletal muscles.
- Temperature adaptation influences enzyme structure and function, impacting metabolic efficiency.
Purpose:
- To investigate how adaptation to low and high environmental temperatures affects the kinetic and structural properties of fish skeletal muscle lactate dehydrogenase (LDH).
- To compare the thermal and urea-induced stability of LDH from fishes adapted to different temperature regimes.
- To explore the reversibility of temperature-induced changes in LDH properties.
Summary:
- Fishes adapted to low temperatures exhibit LDH with a lower optimal temperature for pyruvate binding (KM) and increased stability against thermal and urea denaturation.
- Fishes adapted to high temperatures show LDH with a higher optimal temperature for pyruvate binding and reduced stability.
- Treatment with urea and subsequent reactivation eliminates the observed differences in kinetic properties between LDH from cold- and warm-adapted fish.
Impact:
- Understanding enzyme adaptation mechanisms provides insights into organismal resilience to climate change.
- Reveals how environmental factors shape protein structure-function relationships.
- Highlights the plasticity of enzymes like LDH in response to thermal stress.