A vertebrate aldo-keto reductase active with retinoids and ethanol

被引:32
作者
Crosas, B
Cederlund, E
Torres, D
Jörnvall, H
Farrés, J
Parés, X [1 ]
机构
[1] Univ Autonoma Barcelona, Dept Biochem & Mol Biol, E-08193 Bellaterra, Barcelona, Spain
[2] Karolinska Inst, Dept Med Biochem & Biophys, S-17177 Stockholm, Sweden
关键词
D O I
10.1074/jbc.M010478200
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
Enzymes of the short chain and medium chain dehydrogenase/reductase families have been demonstrated to participate in the oxidoreduction of ethanol and retinoids. Mammals and amphibians contain, in the upper digestive tract mucosa, alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, active with ethanol and retinol, In the present work, we searched for a similar enzyme in an avian species (Gallus domesticus), We found that chicken does not contain the homologous enzyme from the medium chain dehydrogenase/reductase family but an oxidoreductase from the aldo-keto reductase family, with retinal reductase and alcohol dehydrogenase activities, The amino acid sequence shows 66-69% residue identity with the aldose reductase and aldose reductase-like enzymes. Chicken aldo-keto reductase is a monomer of M-r 36,000 expressed in eye, tongue, and esophagus. The enzyme can oxidize aliphatic alcohols, such as ethanol, and it is very efficient in all-trans- and 9-cis-retinal reduction (k(cat)/K-m = 5,300 and 32,000 mM(-1).min(-1), respectively). This finding represents the inclusion of the aldo-keto reductase family, with the (alpha/beta)(8) barrel structure, into the scenario of retinoid metabolism and, therefore, of the regulation of vertebrate development and tissue differentiation.
引用
收藏
页码:19132 / 19140
页数:9
相关论文
共 65 条
[1]   BIASED PROBABILITY MONTE-CARLO CONFORMATIONAL SEARCHES AND ELECTROSTATIC CALCULATIONS FOR PEPTIDES AND PROTEINS [J].
ABAGYAN, R ;
TOTROV, M .
JOURNAL OF MOLECULAR BIOLOGY, 1994, 235 (03) :983-1002
[2]   Retinoids, ω-hydroxyfatty acids and cytotoxic aldehydes as physiological substrates, and H2-receptor antagonists as pharmacological inhibitors, of human class IV alcohol dehydrogenase [J].
Allali-Hassani, A ;
Peralba, JM ;
Martras, S ;
Farrés, J ;
Parés, X .
FEBS LETTERS, 1998, 426 (03) :362-366
[3]   RETRACTED: Directed evolution of new catalytic activity using the α/β-barrel scaffold (Retracted article. See vol 417, pg 468, 2002) [J].
Altamirano, MM ;
Blackburn, JM ;
Aguayo, C ;
Fersht, AR .
NATURE, 2000, 403 (6770) :617-622
[4]  
ALTSCHUL SF, 1990, J MOL BIOL, V215, P403, DOI 10.1006/jmbi.1990.9999
[5]   Expression patterns of class I and class IV alcohol dehydrogenase genes in developing epithelia suggest a role for alcohol dehydrogenase in local retinoic acid synthesis [J].
Ang, HL ;
Deltour, L ;
ZgombicKnight, M ;
Wagner, MA ;
Duester, G .
ALCOHOLISM-CLINICAL AND EXPERIMENTAL RESEARCH, 1996, 20 (06) :1050-1064
[6]   Steroid recognition and regulation of hormone action: Crystal structure of testosterone and NADP(+) bound to 3 alpha-hydroxysteroid dihydrodiol dehydrogenase [J].
Bennett, MJ ;
Albert, RH ;
Jez, JM ;
Ma, HC ;
Penning, TM ;
Lewis, M .
STRUCTURE, 1997, 5 (06) :799-812
[7]  
BOHREN KM, 1992, J BIOL CHEM, V267, P20965
[8]   PHYSIOLOGICAL SUBSTRATES FOR RAT ALCOHOL-DEHYDROGENASE CLASSES - ALDEHYDES OF LIPID-PEROXIDATION, OMEGA-HYDROXYFATTY ACIDS, AND RETINOIDS [J].
BOLEDA, MD ;
SAUBI, N ;
FARRES, J ;
PARES, X .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1993, 307 (01) :85-90
[9]   ROLE OF EXTRAHEPATIC ALCOHOL-DEHYDROGENASE IN RAT ETHANOL-METABOLISM [J].
BOLEDA, MD ;
JULIA, P ;
MORENO, A ;
PARES, X .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1989, 274 (01) :74-81
[10]   Identification and characterization of a novel human aldose reductase-like gene [J].
Cao, DL ;
Fan, ST ;
Chung, SSM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (19) :11429-11435