Characterisation of a novel mouse liver aldo-keto reductase AKR7A5.
We have characterised a novel aldo-keto reductase (AKR7A5) from mouse liver that is 78% identical to rat aflatoxin dialdehyde reductase AKR7A1 and 89% identical to human succinic semialdehyde (SSA) reductase AKR7A2. AKR7A5 can reduce 2-carboxybenzaldehyde (2-CBA) and SSA as well as a range of aldehyde and diketone substrates. Western blots show that it is expressed in liver, kidney, testis and brain, and at lower levels in skeletal muscle, spleen heart and lung. The protein is not inducible in the liver by dietary ethoxyquin. Immunodepletion of AKR7A5 from liver extracts shows that it is one of the major liver 2-CBA reductases but that it is not the main SSA reductase in this tissue.
Department of Pharmaceutical Sciences, University of Strathclyde, 204 George Street, G1 1XW, Glasgow, UK.
Alison
A
Hinshelwood
Gail
G
McGarvie
Elizabeth
E
Ellis
D000429:Alcohol Oxidoreductases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000449:Aldehyde Reductase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D000074408:Aldo-Keto Reductases; D000818:Animals; D002384:Catalysis; D003001:Cloning, Molecular; D004790:Enzyme Induction / Q000187:drug effects; D005015:Ethoxyquin / Q000494:pharmacology; D006801:Humans; D006884:Hydroxybutyrate Dehydrogenase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D051379:Mice; D008969:Molecular Sequence Data; D051381:Rats; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D014018:Tissue Distribution; D005680:gamma-Aminobutyric Acid / Q000031:analogs & derivatives / Q000378:metabolism*
D005680:gamma-Aminobutyric Acid; D005015:Ethoxyquin; D000429:Alcohol Oxidoreductases; C442302:AKR7A1; D000074408:Aldo-Keto Reductases; D000449:Aldehyde Reductase; D006884:Hydroxybutyrate Dehydrogenase; C019416:4-hydroxybutyrate dehydrogenase; C000614209:AKR7A5 protein, mouse; C009338:succinic semialdehyde