Evidence for the identity of glutathione-dependent formaldehyde dehydrogenase and class III alcohol dehydrogenase
نویسندگان
چکیده
منابع مشابه
Function, Expression and Polymorphism of Human Alcohol Dehydrogenase 3/Glutathione- Dependent Formaldehyde Dehydrogenase
Alcohol dehydrogenase 3 (ADH3), identical to glutathione-dependent formaldehyde dehydrogenase, plays a vital role in the defense against formaldehyde through the activity for the spontaneously formed adduct between formaldehyde and glutathione, Shydroxymethylglutathione (HMGSH). ADH3 may also participate in the metabolism of S-nitrosylated glutathione, GSNO. To further investigate substrate enz...
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The ADH2 gene codes for the Arabidopsis glutathione-dependent formaldehyde dehydrogenase (FALDH), an enzyme involved in formaldehyde metabolism in eukaryotes. In the present work, we have investigated the potential role of FALDH in detoxification of exogenous formaldehyde. We have generated a yeast (Saccharomyces cerevisiae) mutant strain (sfa1Delta) by in vivo deletion of the SFA1 gene that co...
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The distributions of class III alcohol dehydrogenase (ADH), a glutathione-dependent formaldehyde dehydrogenase, and class I ADH in the human brain were examined immunohistochemically. The most intense immunostaining of class III ADH was observed in the dendrites and cytoplasm of cerebellar Purkinje cells. Scattered cerebral cortical neurons in layers IV and V, and some hippocampal pyramidal neu...
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The origin of the fatty acid activation and formaldehyde dehydrogenase activity that distinguishes human class III alcohol dehydrogenase (alcohol:NAD+ oxidoreductase, EC 1.1.1.1) from all other alcohol dehydrogenases has been examined by site-directed mutagenesis of its Arg-115 residue. The Ala- and Asp-115 mutant proteins were expressed in Escherichia coli and purified by affinity chromatograp...
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The results obtained led the authors to the suggestion that Reactions 2 and 4 are catalyzed by liver alcohol dehydrogenase but that Reaction 1 is due to an aldehyde dehydrogenase present in their liver preparation. Because of the inhomogeneity of the enzyme preparation employed, a reinvestigation of this problem with more highly purified enzyme was suggested. With the use of crystalline horse l...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1989
ISSN: 0014-5793
DOI: 10.1016/0014-5793(89)81797-1