Abstract
Formaldehyde is oxidized in mammalian tissues and in several other sources to formate in two consecutive reactions catalyzed by separate enzymes (Uotila and Koivusalo, 1974a; 1974b) (Scheme 1). Formaldehyde and glutathione react first non-enzymically to form a hemithioacetal adduct (S-hydroxymethylglutathione) (Reaction 1). The adduct is the substrate of formaldehyde dehydrogenase (EC 1.2.1.1) and is oxidized in the NAD-depend-ent reaction to S-formylglutathione (Reaction 2). Formaldehyde dehydrogenase has been shown to be identical with the class III alcohol dehydrogenase (Koivusalo et al., 1989). For a comprehensive review on formaldehyde dehydrogenase, see Uotila and Koivusalo (1989). The hydrolysis of S-formylglutathione to reduced glutathione and formate (Reaction 3) is catalyzed by a specific enzyme, S-formylglutathione hydrolase (EC 3.1.2.12). Formate can be oxidized by the catalase reaction or is transferred to tetrahydrofolate to form 10-formyl-tetrahydrofolate. Formate is thus incorporated into the reactions of the C-1 metabolism by which it can be oxidized to carbon dioxide in the 10-tetrahydrofolate dehydrogenase reaction (Kutzbach and Stokstad, 1968).
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Koivusalo, M., Lapatto, R., Uotila, L. (1995). Purification and Characterization of S-Formylglutathione Hydrolase from Human, Rat and Fish Tissues. In: Weiner, H., Holmes, R.S., Wermuth, B. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 5. Advances in Experimental Medicine and Biology, vol 372. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1965-2_50
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DOI: https://doi.org/10.1007/978-1-4615-1965-2_50
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