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.

Automated summary

New research finds that the enzymatic oxidation of ethanol is significantly accelerated by ADH1A alcohol dehydrogenase in the presence of ATP, by up to 20 times. This challenges the previous understanding of the role of ATP in ADH enzyme function and calls for a thorough revision of existing literature on ADH enzyme properties.