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Proc Natl Acad Sci U S A. 2015 Jan 13;112(2):458-63. doi: 10.1073/pnas.1404167111. Epub 2014 Dec 1.

Hominids adapted to metabolize ethanol long before human-directed fermentation.

Author information

1
Department of Natural Sciences, Santa Fe College, Gainesville, FL 32606; Foundation for Applied Molecular Evolution, Gainesville, FL 32604; and matthew.carrigan@sfcollege.edu.
2
Foundation for Applied Molecular Evolution, Gainesville, FL 32604; and.
3
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN 46202.

Abstract

Paleogenetics is an emerging field that resurrects ancestral proteins from now-extinct organisms to test, in the laboratory, models of protein function based on natural history and Darwinian evolution. Here, we resurrect digestive alcohol dehydrogenases (ADH4) from our primate ancestors to explore the history of primate-ethanol interactions. The evolving catalytic properties of these resurrected enzymes show that our ape ancestors gained a digestive dehydrogenase enzyme capable of metabolizing ethanol near the time that they began using the forest floor, about 10 million y ago. The ADH4 enzyme in our more ancient and arboreal ancestors did not efficiently oxidize ethanol. This change suggests that exposure to dietary sources of ethanol increased in hominids during the early stages of our adaptation to a terrestrial lifestyle. Because fruit collected from the forest floor is expected to contain higher concentrations of fermenting yeast and ethanol than similar fruits hanging on trees, this transition may also be the first time our ancestors were exposed to (and adapted to) substantial amounts of dietary ethanol.

KEYWORDS:

alcohol dehydrogenase; ethanol; evolution; experimental paleogenetics; primates

Comment in

PMID:
25453080
PMCID:
PMC4299227
DOI:
10.1073/pnas.1404167111
[Indexed for MEDLINE]
Free PMC Article

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