| Name | alcohol dehydrogenase 3 |
|---|---|
| Synonyms | ADH1C; ADH3; Alcohol dehydrogenase 1C; Alcohol dehydrogenase 3; Alcohol dehydrogenase gamma subunit; Alcohol dehydrogenase 1Cs; Alcohol dehydrogenase 3s; Alcohol dehydrogenase gamma subunits |
| Name | formaldehyde |
|---|---|
| CAS | formaldehyde |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 19460944 | Thompson CM, Sonawane B, Grafstrom RC: The ontogeny, distribution, and regulation of alcohol dehydrogenase 3: implications for pulmonary physiology. Drug Metab Dispos. 2009 Aug;37(8):1565-71. Epub 2009 May 21. Consideration of ADH3 function relative to the respiratory effects of formaldehyde, as well as to other chemical and biological exposures that might act in an additive or synergistic manner with formaldehyde, might be critical to gain better insight into the association between formaldehyde exposure and childhood asthma. |
121(1,2,3,6) | Details |
| 18097950 | Thompson CM, Grafstrom RC: Mechanistic considerations for formaldehyde-induced bronchoconstriction involving S-nitrosoglutathione reductase. J Toxicol Environ Health A. 2008;71(3):244-8. Recent studies on asthma and airway biology implicate changes in (NO) disposition in the adverse effects of formaldehyde, principally because enzymatic reduction of the endogenous bronchodilator S-nitrosoglutathione (GSNO) is dependent upon GSNO reductase (formally designated as alcohol dehydrogenase-3, ADH3), which also serves as the primary enzyme for cellular detoxification of formaldehyde. |
113(1,2,2,3) | Details |
| 19011746 | Staab CA, Hellgren M, Hoog JO: 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. Cell Mol Life Sci. 2008 Dec;65(24):3950-60. By oxidation of HMGSH, the spontaneous adduct of formaldehyde, ADH3 is implicated in the detoxification of formaldehyde. |
85(1,1,1,5) | Details |
| 19038239 | Staab CA, Alander J, Morgenstern R, Grafstrom RC, Hoog JO: The Janus face of alcohol dehydrogenase 3. . Chem Biol Interact. 2009 Mar 16;178(1-3):29-35. Epub 2008 Nov 6. Mammalian alcohol dehydrogenase 3 (ADH3) represents the key enzyme in the formaldehyde detoxification pathway by oxidation of S-hydroxymethylglutathione [HMGSH; the (GSH) adduct of formaldehyde]. |
66(0,2,2,6) | Details |
| 19697421 | Speit G, Neuss S, Schmid O: The human lung cell line A549 does not develop adaptive protection against the DNA-damaging action of formaldehyde. Environ Mol Mutagen. 2009 Aug 20. |
0(0,0,0,0) | Details |
| 19489444 | Haseba T: [A new sight on alcohol metabolism and alcoholism--role of high Km alcohol dehydrogenase ADH3 (Class III)]. Nihon Arukoru Yakubutsu Igakkai Zasshi. 2009 Apr;44(2):78-93. Recently, we used ADH3-null mutant mice to demonstrate that high Km ADH3 (Class III), a ubiquitous enzyme of ancient origin, contributes to systemic metabolism dose-dependently resulting in a diminution of acute alcohol intoxication. |
11(0,0,0,11) | Details |
| 18412547 | Staab CA, Alander J, Brandt M, Lengqvist J, Morgenstern R, Grafstrom RC, Hoog JO: Reduction of S-nitrosoglutathione by alcohol dehydrogenase 3 is facilitated by substrate via direct cofactor recycling and leads to GSH-controlled formation of glutathione transferase inhibitors. Biochem J. 2008 Aug 1;413(3):493-504. The adduct of formaldehyde, HMGSH (S-hydroxymethylglutathione), was oxidized with a k (cat)/K (m) value approx. 10 times the k (cat)/K (m) value of GSNO reduction, as determined by fluorescence spectroscopy. |
2(0,0,0,2) | Details |