Characterisation of a novel mouse liver aldo-keto reductase AKR7A5
| Autor: | Elizabeth M. Ellis, Gail McGarvie, Alison Hinshelwood |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
7-Dehydrocholesterol reductase
Molecular Sequence Data Biophysics Aldo-Keto Reductases Spleen Biology Reductase Biochemistry Catalysis Succinic semialdehyde Substrate Specificity chemistry.chemical_compound Hydroxybutyrate Dehydrogenase Mice Ethoxyquin Structural Biology Aldehyde Reductase Genetics medicine Animals Humans Tissue Distribution Mouse liver Cloning Molecular Molecular Biology gamma-Aminobutyric Acid Kidney Aldo-keto reductase Sequence Homology Amino Acid Skeletal muscle Cell Biology Rats stomatognathic diseases Alcohol Oxidoreductases medicine.anatomical_structure chemistry Carbonyl metabolism Liver Enzyme Induction |
| Zdroj: | FEBS letters. 523(1-3) |
| ISSN: | 0014-5793 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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