Purification and properties of mouse stomach aldehyde dehydrogenase. Evidence for a role in the oxidation of peroxidic and aromatic aldehydes.
The major isozyme of aldehyde dehydrogenase in mouse stomach, AHD-4, has been purified to homogeneity and characterized with a range of aldehyde substrates at pH 7.4. The enzyme was a dimer with a subunit size of 65 kDa. Using V/Km values as an indication of substrate efficacy, aromatic aldehydes were the preferred substrates. The enzyme used either NAD+ or NADP+ as cofactor, but showed a preference for NAD+. AHD-4 showed 'high-Km' properties with respect to acetaldehyde, but differed from the 'high-Km' liver mitochondrial enzyme (AHD-1), in that it was not a semialdehyde dehydrogenase. The enzyme was significantly active towards the peroxidic aldehyde, 4-hydroxynonenal, and may play a role in vivo in the detoxification of aromatic aldehydes and the aldehyde products of lipid peroxidation.
Algar
E M
EM
Division of Science and Technology, Griffith University, Brisbane, Australia.
Holmes
R S
RS
D000079:Acetaldehyde / Q000378:metabolism; D000444:Aldehyde Dehydrogenase / Q000302:isolation & purification* / Q000378:metabolism; D000447:Aldehydes / Q000378:metabolism; D000818:Animals; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D046911:Macromolecular Substances; D051379:Mice; D008810:Mice, Inbred C57BL; D008815:Mice, Inbred Strains; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D013270:Stomach / Q000201:enzymology*; D013379:Substrate Specificity
D000447:Aldehydes; D007527:Isoenzymes; D046911:Macromolecular Substances; D009243:NAD; D009249:NADP; D000444:Aldehyde Dehydrogenase; D000079:Acetaldehyde