Medium- and short-chain dehydrogenase/reductase gene and protein families |
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Authors: | C A Staab M Hellgren J-O Höög |
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Institution: | (1) ToxStrategies, Inc, 23501 Cinco Ranch Blvd, Suite G265, Katy TX 77494, USA;(2) Institute of Environmental Medicine, Karolinska Institutet, SE-171 77 Stockholm, Sweden;(3) Medical Biotechnology, VTT Technical Research Centre of Finland, PO Box 106, FI-20521 Turku, Finland |
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Abstract: | 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. |
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