Medium- and short-chain dehydrogenase/reductase gene and protein families

Dual functions of alcohol dehydrogenase 3: implications with focus on formaldehyde dehydrogenase and S-nitrosoglutathione reductase activities
Multi-author Review

DOI: 10.1007/s00018-008-8592-2

Cite this article as:
Staab, C.A., Hellgren, M. & Höög, JO. Cell. Mol. Life Sci. (2008) 65: 3950. doi:10.1007/s00018-008-8592-2


Alcohol dehydrogenase 3 (ADH3) is highly conserved, ubiquitously expressed in mammals and involved in essential cellular pathways. A large active site pocket entails special substrate specificities: shortchain alcohols are poor substrates, while medium-chain alcohols and particularly the glutathione adducts S-hydroxymethylglutathione (HMGSH) and S-nitrosoglutathione (GSNO) are efficiently converted under concomitant use of NAD+/NADH. By oxidation of HMGSH, the spontaneous glutathione adduct of formaldehyde, ADH3 is implicated in the detoxification of formaldehyde. Through the GSNO reductase activity, ADH3 can affect the transnitrosation equilibrium between GSNO and S-nitrosated proteins, arguing for an important role in NO homeostasis. Recent findings suggest that ADH3-mediated GSNO reduction and subsequent product formation responds to redox states in terms of NADH availability and glutathione levels. Finally, a dual function of ADH3 is discussed in view of its potential implications for asthma.


Alcohol dehydrogenase formaldehyde metabolic interaction S-nitrosoglutathione protein S-nitrosation 

Copyright information

© Birkhäuser Verlag, Basel 2008

Authors and Affiliations

  1. 1.Department of Medical Biochemistry and BiophysicsKarolinska InstitutetStockholmSweden

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