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Hominids adapted to metabolize ethanol long before human-directed fermentation
Matthew A Carrigan1, Oleg Uryasev2, Carole B Frye2
1Department of Natural Sciences, Santa Fe College, Gainesville, FL 32606; Foundation for Applied Molecular Evolution, Gainesville, FL 32604; and matthew.carrigan@sfcollege.edu.
Researchers resurrected ancestral alcohol dehydrogenase (ADH4) enzymes to study primate-ethanol interactions. This revealed that ape ancestors evolved an ethanol-metabolizing enzyme around 10 million years ago, coinciding with a shift to a terrestrial lifestyle.
Area of Science:
- Paleogenetics
- Evolutionary Biology
- Biochemistry
Background:
- Paleogenetics reconstructs ancestral proteins to study evolutionary adaptations.
- Understanding the evolution of enzyme function provides insights into ancestral diets and behaviors.
Purpose of the Study:
- To investigate the evolutionary history of primate-ethanol interactions.
- To determine when digestive alcohol dehydrogenase (ADH4) gained the ability to metabolize ethanol.
Main Methods:
- Resurrection of ancestral ADH4 enzymes from primate fossils.
- Biochemical assays to measure the catalytic properties of resurrected enzymes, specifically their ability to oxidize ethanol.
Main Results:
- Ancestral ADH4 enzymes from arboreal primates inefficiently metabolized ethanol.
- A significant increase in ethanol-metabolizing efficiency was observed in ADH4 from ape ancestors around 10 million years ago.
- This evolutionary change coincided with the adoption of a terrestrial lifestyle and increased consumption of fallen fruit.
Conclusions:
- The evolution of an efficient ethanol-metabolizing ADH4 enzyme in ape ancestors was linked to dietary changes associated with a terrestrial environment.
- This adaptation suggests early hominids were exposed to and adapted to substantial dietary ethanol from fermenting fallen fruits.
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