ADH5 oxidises S-HMGSH to S-FGSH

Stable Identifier
R-HSA-5692237
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
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, Hempel, J, Vallee, BL, Jörnvall, H

Biochemistry 1988
3278908 Rat liver alcohol dehydrogenase of class III. Primary structure, functional consequences and relationships to other alcohol dehydrogenases

Julià, P, Pareś, X, Jörnvall, H

Eur. J. Biochem. 1988
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
S-(hydroxymethyl)glutathione dehydrogenase activity of ADH5:2xZn2+ dimer [cytosol]
Physical Entity
Activity
Orthologous Events
Cross References
Rhea
Authored
Reviewed
Created
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