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

Khmelinskii, Igor; Makarov, Vladimir I.

http://hdl.handle.net/10400.1/19203

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Autores

Khmelinskii, Igor

Makarov, Vladimir I.

Resumo(s)

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.

Palavras-chave

Enzymatic reaction ATP hydrolysis Alcohol dehydrogenase Enzymatic oxidation of alcohol ATP activation of alcohol dehydrogenase

URI

http://hdl.handle.net/10400.1/19203

Editora

Elsevier

DOI

10.1016/j.biochi.2021.11.002

Coleções

FCT2-Artigos (em revistas ou actas indexadas)

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