Characterisation of a novel mouse liver aldo-keto reductase AKR7A5

被引:42
|
作者
Hinshelwood, A
McGarvie, G
Ellis, E
机构
[1] Univ Strathclyde, Dept Pharmaceut Sci, Glasgow G1 1XW, Lanark, Scotland
[2] Bell Coll, Sch Sci & Technol, Hamilton ML3 OJB, Lanark, Scotland
[3] Univ Strathclyde, Dept Biosci, Glasgow G1 1XW, Lanark, Scotland
来源
FEBS LETTERS | 2002年 / 523卷 / 1-3期
关键词
aldo-keto reductase; succinic semialdehyde; mouse liver; carbonyl metabolism;
D O I
10.1016/S0014-5793(02)02982-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码:213 / 218
页数:6
相关论文
共 50 条
  • [21] Structural characterization of an aldo-keto reductase (AKR2E5) from the silkworm Bombyx mori
    Yamamoto, Kohji
    Higashiura, Akifumi
    Suzuki, Mamoru
    Shiotsuki, Takahiro
    Sugahara, Ryohei
    Fujii, Takeshi
    Nakagawa, Atsushi
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2016, 474 (01) : 104 - 110
  • [22] The role of a mouse aldo-keto reductase in resistance to toxic aldehydes and ketones
    Li, D
    Ellis, E
    TOXICOLOGY, 2004, 202 (1-2) : 77 - 77
  • [23] Structural and mutational studies on an aldo-keto reductase AKR5C3 from Gluconobacter oxydans
    Liu, Xu
    Wang, Chao
    Zhang, Lujia
    Yao, Zhiqiang
    Cui, Dongbing
    Wu, Liang
    Lin, Jinping
    Yuan, Yu-Ren Adam
    Wei, Dongzhi
    PROTEIN SCIENCE, 2014, 23 (11) : 1540 - 1549
  • [24] DAUNORUBICIN (D) AND ADRIAMYCIN (A) REDUCTASE - ALDO-KETO REDUCTASE
    FELSTED, RL
    BACHUR, NR
    FEDERATION PROCEEDINGS, 1974, 33 (05) : 1382 - 1382
  • [25] Enzymatic properties of a member (AKR1C20) of the aldo-keto reductase family
    Matsumoto, K
    Endo, S
    Ishikura, S
    Matsunaga, T
    Tajima, K
    El-Kabbani, O
    Hara, A
    BIOLOGICAL & PHARMACEUTICAL BULLETIN, 2006, 29 (03) : 539 - 542
  • [26] The aldo-keto reductase AKR1B7 coexpresses with renin without influencing renin production and secretion
    Machura, Katharina
    Iankilevitch, Elina
    Neubauer, Bjoern
    Theuring, Franz
    Kurtz, Armin
    AMERICAN JOURNAL OF PHYSIOLOGY-RENAL PHYSIOLOGY, 2013, 304 (05) : F578 - F584
  • [27] Introduction and overview of the Aldo-Keto Reductase superfamily
    Penning, TM
    ALDO-KETO REDUCTASES AND TOXICANT METABOLISM, 2004, 865 : 3 - 20
  • [28] Detoxication of the environmental pollutant acrolein by a rat liver aldo-keto reductase
    Gardner, R
    Kazi, S
    Ellis, EM
    TOXICOLOGY LETTERS, 2004, 148 (1-2) : 65 - 72
  • [29] Regulation Network and Prognostic Significance of Aldo-Keto Reductase (AKR) Superfamily Genes in Hepatocellular Carcinoma
    Dai, Tianxing
    Ye, Linsen
    Yu, Haoyuan
    Li, Kun
    Li, Jing
    Liu, Rongqiang
    Lu, Xu
    Deng, Mingbin
    Li, Rong
    Liu, Wei
    Yang, Yang
    Wang, Guoying
    JOURNAL OF HEPATOCELLULAR CARCINOMA, 2021, 8 : 997 - 1021
  • [30] Pharmacogenetics of aldo-keto reductase 1C (AKR1C) enzymes
    Alshogran, Osama Y.
    EXPERT OPINION ON DRUG METABOLISM & TOXICOLOGY, 2017, 13 (10) : 1063 - 1073