The aldo-keto reductase (AKR) superfamily: an update

被引:212
|
作者
Jez, JM
Penning, TM
机构
[1] Univ Penn, Sch Med, Dept Pharmacol, Philadelphia, PA 19104 USA
[2] Salk Inst Biol Studies, Struct Biol Lab, La Jolla, CA 92037 USA
关键词
aldose-reductase; aldehyde reductase; hydroxysteroid dehydrogenase; oxidoreductases;
D O I
10.1016/S0009-2797(00)00295-7
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
The aldo-keto reductases (AKRs) are one of three enzyme superfamilies encompassing a range of oxidoreductases. Members of the AKR superfamily are monomeric (alpha/beta)(8)-barrel proteins, about 320 amino acids in length, which bind NAD(P)(H) to metabolize an array of substrates. AKRs have been identified in vertebrates, invertebrates, plants, protozoa, fungi, eubacteria, and archaebacteria, implying that this is an ancient superfamily of enzymes. Earlier, in an attempt to clarify the confusion caused by multiple names for particular AKRs, we proposed a systematic and expandable nomenclature system to assign consistent designations to unique members of the AKR superfamily. Since then, the number of characterized AKRs has expanded to 105 proteins in 12 families. In addition, molecular cloning and genome sequencing projects have identified 125 potential AKR genes, many of which have no assigned function. The nomenclature system for the AKR superfamily is accepted by the Human Genome Project. Using the earlier described nomenclature system, we now provide an updated listing of AKRs and potential superfamily members. Information is also available at http://www.med.upenn.edu/akr. (C) 2001 Elsevier Science Ireland Ltd. All rights reserved.
引用
收藏
页码:499 / 525
页数:27
相关论文
共 50 条
  • [31] Metabolism of the synthetic progestogen norethynodrel by human ketosteroid reductases of the aldo-keto reductase superfamily
    Jin, Yi
    Duan, Ling
    Chen, Mo
    Penning, Trevor M.
    Kloosterboer, HeleniusJ.
    JOURNAL OF STEROID BIOCHEMISTRY AND MOLECULAR BIOLOGY, 2012, 129 (3-5): : 139 - 144
  • [32] DAUNORUBICIN (D) AND ADRIAMYCIN (A) REDUCTASE - ALDO-KETO REDUCTASE
    FELSTED, RL
    BACHUR, NR
    FEDERATION PROCEEDINGS, 1974, 33 (05) : 1382 - 1382
  • [33] 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
  • [34] Pharmacogenetics of aldo-keto reductase 1C (AKR1C) enzymes
    Alshogran, Osama Y.
    EXPERT OPINION ON DRUG METABOLISM & TOXICOLOGY, 2017, 13 (10) : 1063 - 1073
  • [35] Enzymatic properties of a member (AKR1C19) of the aldo-keto reductase family
    Ishikura, S
    Horie, K
    Sanai, M
    Matsumoto, K
    Hara, A
    BIOLOGICAL & PHARMACEUTICAL BULLETIN, 2005, 28 (06) : 1075 - 1078
  • [36] Role of Aldo-Keto Reductase (AKR) 1B10 in Human Lung Carcinogenesis
    Quinn, Amy M.
    Harvey, Ronald G.
    Penning, Trevor M.
    CHEMICAL RESEARCH IN TOXICOLOGY, 2008, 21 (12) : 2448 - 2448
  • [37] Characterization of a novel murine aldo-keto reductase
    Bohren, KM
    Barski, OA
    Gabbay, KH
    ENZYMOLOGY AND MOLECULAR BIOLOGY OF CARBONYL METABOLISM 6, 1997, 414 : 455 - 464
  • [38] Structural studies of aldo-keto reductase inhibition
    Wilson, DK
    Nakano, T
    Petrash, JM
    Quiocho, FA
    ENZYMOLOGY AND MOLECULAR BIOLOGY OF CARBONYL METABOLISM 6, 1997, 414 : 435 - 442
  • [39] Aldo-keto Reductase 1B15 (AKR1B15) A MITOCHONDRIAL HUMAN ALDO-KETO REDUCTASE WITH ACTIVITY TOWARD STEROIDS AND 3-KETO-ACYL-CoA CONJUGATES
    Weber, Susanne
    Salabei, Joshua K.
    Moeller, Gabriele
    Kremmer, Elisabeth
    Bhatnagar, Aruni
    Adamski, Jerzy
    Barski, Oleg A.
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2015, 290 (10) : 6531 - 6545
  • [40] Cloning and characterization of human testis specific protein, a novel member of the aldo-keto reductase superfamily
    Azuma, Y
    Ushijima, S
    Soh, J
    Nishinaka, T
    Yabe, C
    Miki, T
    JOURNAL OF UROLOGY, 2002, 167 (04): : 322 - 322