Formaldehyde Dehydrogenase from Yeast and Plant
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Publisher
Springer US
Link
http://link.springer.com/content/pdf/10.1007/978-1-4615-5871-2_43
Reference18 articles.
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2. Boleda, M.D., Saubi, N., Farrés, J. and Parés, X.: Physiological substrates for rat alcohol dehydrogenase classes: Aldehydes of lipid peroxidation, ω-hydroxyfatty acids, and retinoids. Arch. Biochem. Biophys. 307 (1993) 85–90.
3. Engeland, K., Höög, J.O., Holmquist, B., Estonius, M., Jörnvall, H. and Vallee, B.L.: Mutation of Arg-115 of human class III alcohol dehydrogenase: A binding site required for formaldehyde dehydrogenase activity and fatty acid activation. Proc. Natl. Acad. Sci. USA. 90 (1993) 2491–2494.
4. Fan, F. and Plapp, B.V.: Substitutions of isoleucine residues at the adenine binding site activate horse liver alcohol dehydrogenase. Biochemistry 34 (1995) 4709–4713
5. Fernández, M.R., Biosca, J.A., Norin, A., Jörnvall, H. and Parés, X.: Class III alcohol dehydrogenase from Saccharomyces cerevisiae: Structural and enzymatic features differ toward the human/mammalian forms in a manner consistent with functional needs in formaldehyde detoxication. FEBS Lett. 370 (1995) 23–26.
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