ADH5 oxidises S-HMGSH to S-FGSH

Stable Identifier
R-HSA-5692237
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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Alcohol dehydrogenase class-3 (ADH5) is a cytosolic dimeric enzyme that binds 2 Zn2+ per subunit. It is very ineffective in oxidising ethanol, but it readily catalyses the oxidation of S-(hydroxymethyl) glutathione (S-HMGSH) to S-formylglutathione (S-FGSH) (Kaiser et al. 1988, Julia et al. 1988) as well as the oxidation of long-chain primary alcohols (not shown here).
Literature References
PubMed ID Title Journal Year
3278908 Rat liver alcohol dehydrogenase of class III. Primary structure, functional consequences and relationships to other alcohol dehydrogenases

Pareś, X, Jörnvall, H, Julià, P

Eur. J. Biochem. 1988
3365377 Class III human liver alcohol dehydrogenase: a novel structural type equidistantly related to the class I and class II enzymes

Kaiser, R, Holmquist, B, Jörnvall, H, Vallee, BL, Hempel, J

Biochemistry 1988
Participants
Participates
Catalyst Activity

S-(hydroxymethyl)glutathione dehydrogenase activity of ADH5:2xZn2+ dimer [cytosol]

Orthologous Events
Cross References
Rhea
Authored
Reviewed
Created
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