CATH Classification

Domain Context

CATH Clusters

Superfamily NAD(P)-binding Rossmann-like Domain
Functional Family S-(hydroxymethyl)glutathione dehydrogenase

Enzyme Information

With NAD(+) or NADP(+) as acceptor.
based on mapping to UniProt P11766
Alcohol dehydrogenase.
based on mapping to UniProt P11766
(1) A primary alcohol + NAD(+) = an aldehyde + NADH. (2) A secondary alcohol + NAD(+) = a ketone + NADH.
-!- Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. -!- The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
S-(hydroxymethyl)glutathione dehydrogenase.
based on mapping to UniProt P11766
S-(hydroxymethyl)glutathione + NAD(P)(+) = S-formylglutathione + NAD(P)H.
-!- The substrate, S-(hydroxymethyl)glutathione, forms spontaneously from glutathione and formaldehyde; its rate of formation is increased in some bacteria by the presence of EC -!- Forms part of the pathway that detoxifies formaldehyde, since the product is hydrolyzed by EC -!- Also specifically reduces S-nitrosylglutathione. -!- Formerly EC

UniProtKB Entries (1)

Homo sapiens
Alcohol dehydrogenase class-3

PDB Structure

External Links
Organism Escherichia
Primary Citation
Human glutathione-dependent formaldehyde dehydrogenase. Structures of apo, binary, and inhibitory ternary complexes.
Sanghani, P.C., Robinson, H., Bosron, W.F., Hurley, T.D.