Characterisation of a novel mouse liver aldo‐keto reductase AKR7A5

FEBS Letters

Ellis, Elizabeth¹  Hinshelwood, Alison¹  McGarvie, Gail² 

[1] Department of Pharmaceutical Sciences, University of Strathclyde, 204 George Street, Glasgow G1 1XW, UK;School of Science and Technology, Bell College, Almada Street, Hamilton, Lanarkshire ML3 OJB, UK

关键词: Aldo-keto reductase;    Succinic semialdehyde;    Mouse liver;    Carbonyl metabolism;    AKR;    aldo-keto reductase;    SSA;    succinic semialdehyde;    GHB;    γ-hydroxybutyrate;    2-CBA;    2-carboxybenzaldehyde;    4-NBA;    4-nitrobenzaldehyde;    GST;    glutathione S-transferase;    9;    10-PQ;    9;    10-phenanthrenequinone;    NQO1;    NAD(P)H:quinone oxidoreductase;    GABA;    γ-aminobutyrate;   

DOI  :  10.1016/S0014-5793(02)02982-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown