CATH Classification

Domain Context

CATH Clusters

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

Enzyme Information

1.1.1.-
With NAD(+) or NADP(+) as acceptor.
based on mapping to UniProt P11766
1.1.1.1
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.
1.1.1.284
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 4.4.1.22. -!- Forms part of the pathway that detoxifies formaldehyde, since the product is hydrolyzed by EC 3.1.2.12. -!- Also specifically reduces S-nitrosylglutathione. -!- Formerly EC 1.2.1.1.

UniProtKB Entries (1)

P11766
ADHX_HUMAN
Homo sapiens
Alcohol dehydrogenase class-3

PDB Structure

PDB 1MP0
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structure-function relationships in human Class III alcohol dehydrogenase (formaldehyde dehydrogenase)
Sanghani, P.C., Robinson, H., Bennett-Lovsey, R., Hurley, T.D., Bosron, W.F.
Chem.Biol.Interact.