Contrary to consensus, oxidation of ethanol by human alcohol dehydrogenase (ADH) 1A is activated by ATP.

Presently we report that enzymatic oxidation of ethanol (EtOH) by ADH1A alcohol dehydrogenase is strongly accelerated in presence of adenosine triphosphate (ATP), by up to the factor of 20 in vitro. This result provides a different look on the role of ATP in functioning of alcohol dehydrogenases (ADH), which until presently were a textbook example of enzymes not requiring ATP and successfully operating without it. However, ATP is available in every living cell and will activate reactions conducted by ADH enzymes in vivo. Therefore, the body of published literature describing properties of numerous ADH enzymes requires a thorough revision. Process (A) is the textbook spontaneous enzymatic oxidation of ethanol, producing acetaldehyde, while process (B) is ATP-activated enzymatic oxidation of ethanol. The rate of process (B) is much faster than that of process (A) and will dominate in vivo. [Display omitted] • It was found that ATP accelerates enzyme oxidation rate of ethanol. • ATP-sensitized ethanol oxidation by ADH1A was faster by up to the factor of 20 than spontaneous oxidation. • These results contradict the consensus nation that ADH enzymes do not need ATP. [ABSTRACT FROM AUTHOR]