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Enzymogenesis of Zinc‐Dependent Alcohol Dehydrogenases and Aldehyde Dehydrogenases in Animals Show That Their Origin Predates Natural Availability of Ethanol from the Diet
Author(s) -
JuliánSánchez Adriana,
HernándezTobías Aída,
VaraCisneros Paola,
GaonaLópez Carlos,
AlvaradoLeaño Juan,
Piña Enrique,
RiverosRosas Hector
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.lb163
Subject(s) - acetaldehyde , aldehyde dehydrogenase , alcohol dehydrogenase , ethanol , enzyme , biochemistry , yeast , biology , alcohol , ethanol metabolism , chemistry , botany
In vertebrates, ethanol metabolism is performed through the concerted action of two enzymes: a Zn‐dependent alcohol dehydrogenase (Zn‐ADH) that oxidizes ethanol to acetaldehyde, and an aldehyde dehydrogenase (ALDH) that oxidizes acetaldehyde to acetate. The presence of these Zn‐ADHs and several ALDHs in animals has been assumed to be a consequence of chronic ethanol exposure from the diet. The main natural source of ethanol is fermentation of fruit sugars by yeast. The origin of angiosperms with fleshy fruits dates from the Lower Cretaceous (130‐140 million years ago). Because association between yeast and angiosperms dates also from the Cretaceous, dietary exposure of diverse frugivorous taxa to ethanol is similarly ancient. Since substrate availability must precede enzyme selection, then it can be expected that the enzymogenesis of the ADHs/ALDHs began after the appearance of fleshy fruits. Phylogenetic analyses reveal that all different Zn‐ADHs (seven classes) in animals appeared before land plants, independently of ethanol availability. With respect to aldehyde dehydrogenases (ALDH), phylogenetic analyses showed 13 different ALDH families in animals, and all they appeared before land plants. Because all these enzymes are not induced by ethanol and possess a high activity with non‐ethanol endogenous substrates, it can be concluded that Zn‐ADH and ALDH participation in ethanol metabolism can be considered as incidental, and not adaptive. Supported by DGAPA‐UNAM grant IN216513.