Journal of Molecular Evolution

, Volume 28, Issue 1–2, pp 145–150 | Cite as

Alcohol dehydrogenase polymorphism inDrosophila: Enzyme kinetics of product inhibition

  • Pieter W. H. Heinstra
  • Willem Scharloo
  • George E. W. Thorig


Because natural populations ofDrosophila melanogaster are polymorphic for different allozymes of alcohol dehydrogenase (ADH) and becauseD. melanogaster is more tolerant to the toxic effects of ethanol than its sibling speciesD. simulans, information regarding the sensitivities of the different forms of ADH to the products of ethanol degradation are of ecological importance. ADH-F, ADH-S, ADH-71k ofD. melanogaster and the ADH ofD. simulans were inhibited by NADH, but the inhibition was relieved by NAD+. The order of sensitivity of NADH was ADH-F<ADH-71k, ADH-S<ADH-simulans with ADH-F being about four times less sensitive than theD. melanogaster enzymes and 12 times less sensitive than theD. simulans enzyme. Acetaldehyde inhibited the ethanolto-acetaldehyde activity of the ADHs, but at low acetaldehyde concentrations ethanol and NAD+ reduced the inhibition. ADH-71k and ADH-F were more subject to the inhibitory action of acetaldehyde than ADH-S and ADH-simulans, with ADH-71k being seven times more sensitive than ADH-S. The pattern of product inhibition of ADH-71k suggests a rapid equilibrium random mechanism for ethanol oxidation. Thus, although the ADH variants only differ by a few amino acids, these differences exert a far larger impact on their intrinsic properties than previously thought. How differences in product inhibition may be of significance in the evolution of the ADHs is discussed.

Key words

Alcohol dehydrogenase Drosophila Enzyme kinetics Product inhibition Microevolution 


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Copyright information

© Springer-Verlag New York Inc. 1988

Authors and Affiliations

  • Pieter W. H. Heinstra
    • 1
  • Willem Scharloo
    • 1
  • George E. W. Thorig
    • 1
  1. 1.Department of Population and Evolutionary BiologyUniversity of Utrecht Padualaan 8UtrechtThe Netherlands

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