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A Nomenclature System for the Aldo-Keto Reductase Superfamily

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Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 414)

Abstract

The aldo-keto reductases (AKRs) represent a growing superfamily of oxidoreductases (Bohren et al., 1989; Bruce et al., 1994). Proteins of the AKR superfamily are monomeric (α/β)8-barrel proteins, about 320 amino acids in length, which bind NAD(P)(H) without a Rossmann-fold motif (Rondeau et al., 1992; Wilson et al., 1992 > 1995; Hoog et al., 1994, El-Kabbani et al., 1995). Found in mammals, amphibians, plants, yeast, protozoa, and bacteria, the AKRs metabolize a range of substrates including aliphatic aldehydes, monosaccharides, steroids, prostaglandins, polycyclic aromatic hydrocarbons, and isoflavinoid phytoalexins. To date, at least thirty-nine proteins have been cloned and characterized as members of the superfamily, and additional genes have been identified that potentially code for AKR proteins. The rapid progress in identifying new AKRs has lead to some problem in the naming of these proteins.

Keywords

Aldose Reductase Xylose Reductase Nomenclature System Pichia Stipitis Hydroxysteroid Dehydrogenase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References

  1. Altschul, S.F., Gish, W., Miller, W., Myers, E.W., & Lipman, D.J. (1990) Basic local alignment search tool. J. Mol. Biol 215:403–410PubMedGoogle Scholar
  2. Amore, R., Kotter, P., Kuster, C., Ciriacy, M., & Hollenberg, C.P. (1991) Cloning and expression in Saccharomyces cerevisiae of the NAD(P)H-dependent xylose reductase encoding gene (XYL1) from the xylose-assimilating yeast Pichia stipitis. Gene 109: 89–97PubMedCrossRefGoogle Scholar
  3. Anderson, S., Berman-Marks, C., Lazarus, R., Miller, J., Stafford, K., Seymour, J., Light, D., Rastetter, W., & Estell, D. (1985) Production of 2-keto-L-gulonate, an intermediate in L-ascorbate synthesis, by a genetically modified Erwinia herbicola. Science 230: 144–149PubMedCrossRefGoogle Scholar
  4. Bartels, D., Engelhardt, K., Roncarati, R., Schneider, K., Rutts, M., & Salamini, F. (1991) An ABA and GA modulated gene expressed in the barley embryo encodes an aldose reductase related protein. EMBO J. 10: 1037–1043PubMedGoogle Scholar
  5. Billard, P.P., Menait, S.S., Fleer, R.R., & Bolotin-Fukuhara, M.M. (1994) Isolation and characterization of the gene encoding xylose reductase from Kluyveromyces lactis. Gene 162: 93–97CrossRefGoogle Scholar
  6. Bohren, K.M., Bullock, B., Wermuth, B., & Gabbay, K.H. (1989) The aldo-keto reductase superfamily J. Biol. Chem. 264:9547–9551PubMedGoogle Scholar
  7. Bruce, N.C., Willey, D.L., Coulson, A.F.W., & Jeffrey, J. (1994) Bacterial morphine dehydrogenase further defines a distinct superfamily of oxidoreductases with diverse functional activities. Biochem. J. 299: 805–811PubMedGoogle Scholar
  8. Carper, D., Nishimura, C., Shinohara, T., Dietzchold, B., Wistow, G., Craft, C., Kador, P., & Kinoshita, J.H. (1987) Aldose reductase and ρ-crystallin belong to the same protein superfamily as aldehyde reductse. FEBS Letters 220: 209–213PubMedCrossRefGoogle Scholar
  9. Del Bello, B., Maellaro, E., Sugherini, L., Santucci, A., Comporti, M., & Casini, A.F. (1994) Purification of NADPH-dependent dehydroascorbate reductase from rat liver and its identification with 3α-hydroxysteroid dehydrogenase. Biochem. J. 304: 385–390PubMedGoogle Scholar
  10. Devereux, J., Haeberil, P., & Smithies, O. (1984) A comprehensive set of sequence analysis programs for the VAX. Nucleic. Acids Res. 12: 387–395PubMedCrossRefGoogle Scholar
  11. Deyashiki, Y., Ohshima, K., Nakanishi, M., Sato, K., Matsuura, K., & Hara, A. (1995) Molecular cloning and characterization of mouse estradiol 17β-dehydrogenase (A-specific), a member of the aldo-keto reductase family. J. Biol. Chem. 270: 10461–10467PubMedCrossRefGoogle Scholar
  12. Donohue, P.J., Alberts, G.F., Hampton, B.S. & Winkles, J.A. (1994) A delayed-early gene activated by fibroblast growth factor-1 encodes a protein related to aldose reductase. J. Biol. Chem. 269: 8604–8609PubMedGoogle Scholar
  13. El-Kabbani, I., Judge, K., Ginell, S.L., Myles, D.A.A., DeLucas, L.J., & Flynn, T.G. (1995) Structure of porcine aldehyde reductase holoenzyme. Nature Structural Biology 2: 687–692PubMedCrossRefGoogle Scholar
  14. Ellis, E.M., Judah, D.J., Neal, G.E., & Hayes, J.D. (1993) An ethoxyquin-inducible aldehyde reductase from rat liver that metabolizes aflatoxin Bl defines a subfamily of the aldo-keto reductases. Proc. Natl. Acad. Sci. USA 90: 10350–10354PubMedCrossRefGoogle Scholar
  15. Farber, G.K. & Petsko, G.A. (1990) The evolution of α/β-barrel enzymes. Trends in Biochem. Sciences 15: 228–234CrossRefGoogle Scholar
  16. Flynn, T.G., Green, N.C., Bhatia, M.B., & El-Kabbani, O. (1995) Structure and mechanism of aldehyde reductase Adv. Exp. Med. & Bio. 372: 193–201CrossRefGoogle Scholar
  17. Garcia-Perez, A., Martin, B., Murphy, H.R., Uchida, S., Murer, H., Cowley, B.D., Handler, J.S., & Burg, M.B. (1989) Molecular cloning of cDNA coding for kidney aldose reductase. J. Biol. Chem. 264: 16815–16821PubMedGoogle Scholar
  18. Gish, W. & States, D.J. (1993) Identification of protein coding regions by database similarity search. Nature Genetics 3: 266–272PubMedCrossRefGoogle Scholar
  19. Grindley, J.G., Payton, M.A., De Pol, H., & Hardy, K.G. (1988) Conversion of glucose to 2-keto-L-gulonate, an intermediate in L-ascorbate synthesis, by a recombinant strain of Erwinia citreus. Appl. Environ. Microbiol. 54: 1770–1775PubMedGoogle Scholar
  20. Gui, T., Tanimoto, T., Kokai, Y., & Nishimura, C. (1995) Presence of a closely related subgroup in the aldo-keto reductase superfamily of the mouse. Eur. J. Biochem. 227: 448–453PubMedCrossRefGoogle Scholar
  21. Hara, A., Matsuura, K., Tamada, Y., Sato, K., Miyabe, Y., Deyashiki, Y., & Ishida, N. (1996) Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid binding protein and an oxidoreductase of human colon cells. Biochem. J. 313: 373–376.PubMedGoogle Scholar
  22. Hoog, S.S., Pawlowski, J.E., Alzari, P.M., Penning, T.M., & Lewis, M. (1994) Three-dimensional structure of rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase: a member of the aldo-keto reductase superfamily. Proc. Natl. Acad. Sci. USA 91: 2517–2521PubMedCrossRefGoogle Scholar
  23. Jaquinod, M., Potier, N., Klarskov, K., Reymann, J.M., Sorokine, O., Kieffer, S., Barth, P., Andriantomanga, V., Biellman, J.F., & Van Dorsselaes, A. (1993) Sequence of pig lens aldose reductase and electrospray mass spectroscopy of non-covalent and covalent complexes. Eur. J. Biochem. 218: 893–903PubMedCrossRefGoogle Scholar
  24. Jornvall, H., Persson, M., Krook, M., Atrian, S., Gonzalez-Duarte, R., Jeffrey, J., & Ghosh, D. (1995) Short-chain dehydrogenases/reductases (SDR). Biochemistry 34: 6003–6013PubMedCrossRefGoogle Scholar
  25. Kanayama, Y., Moni, H., Imaseki, H., & Yamaki, S. (1992) Nucleotide sequence of a cDNA encoding NADP-sorbitol-6-phosphate dehydrogenase from apple. Plant Physio. 100: 1607–1608CrossRefGoogle Scholar
  26. Khanna, M., Qin, K.N., Wang, R.W., & Cheng, K.C. (1995) Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3a-hydroxysteroid dehydrogenases. J. Biol. Chem. 270: 20162–20168PubMedCrossRefGoogle Scholar
  27. Kita, K. (1995) Cloning, sequence analysis, and expression of aldehyde reductase from red yeast Sporobolomyces salmonicolor. GenBank submissionGoogle Scholar
  28. Kondo, K., Kai, M., Setoguchi, Y., Eggertsen, G., Sjoblom, P., Setoguchi, T., Okuda, K., & Bjorkhem, I. (1994) Cloning and expression of cDNA of human Δ4-3-oxosteroid-5β-reductase and substrate specificity of the expresed enzyme. Eur. J. Biochem. 219: 357–363PubMedCrossRefGoogle Scholar
  29. Lacy, W.R., Washenick, K.J., Cook, R.G., & Dunbar, B.S. (1993) Molecular cloning and expression of an abundant rabbit ovarian protein with 20α-hydroxysteroid dehydrogenase activity. Mol. Endo. 7: 58–66CrossRefGoogle Scholar
  30. Lee, S.P. & Chen, T.H.H. (1993) Molecular cloning of abscisic acid-responsive mRNAs expressed during induction of freezing tolerance in bromegrass suspension culture. Plant Physio. 101: 1089–1092CrossRefGoogle Scholar
  31. McCormack, T. & McCormack, K. (1994) Shaker K+ channel β-subunits belong to an NAD(P)H-dependent oxidoreductase superfamily. Cell 79: 1133–1135PubMedCrossRefGoogle Scholar
  32. Miura, R., Shiota, K., Noda, K., Yagi, S., Ogawa, T., & Takahashi, M. (1994) Molecular cloning of cDNA for rat ovarian 20α-hydroxysteroid dehydrogenase (HSD1). Biochem. J. 299: 561–567PubMedGoogle Scholar
  33. Needleman, S.B. & Wunsch, C.D. (1970) A general method applicable to the search for similarities in the amino acid sequence of two proteins. J. Mol Biol. 48: 443–453PubMedCrossRefGoogle Scholar
  34. Oechsner, U., Magodolen, V., & Bandlow, W. (1988) A nuclear yeast gene (GCY) encodes a polypeptide with high homology to a vertebrate lens protein. FEBS Letters 238: 123–128PubMedCrossRefGoogle Scholar
  35. Onishi, Y., Noshiro, M., Shimosato, T., & Okuda, K. (1994) Molecular cloning and sequence analysis of cDNA encoding Δ4-3-ketosteroid-5β-reductase of rat liver. FEBS Letters 283: 215–218CrossRefGoogle Scholar
  36. Pailhoux, E.A., Martinez, A., Veyssiere, G.M., Jean, C.G. (1990) Androgen-dependent protein from mouse vas deferens. J. Biol. Chem. 265: 19932–19936PubMedGoogle Scholar
  37. Pawlowski, J.E., Huizinga, M., & Penning, T.M. (1991) Cloning and sequencing of the cDNA for rat liver 3α-hydroxysteroid/dihydrodiol dehydrogense. J. Biol. Chem. 266: 8820–8825PubMedGoogle Scholar
  38. Petrash, J.M. & Favello, A.D. (1989) Isolation and characterization of cDNA clones encoding aldose reductase. Exp. Eye Res. 8: 1021–1027Google Scholar
  39. Rettig, J., Heinemann, S.H., Wunder, F., Lorra, C., Parcej, C.N., Dolly, J.O., & Pongs, O. (1994) Inactivation properties of voltage-gated K+ channels altered by presence of beta-subunit. Nature 369: 289–294PubMedCrossRefGoogle Scholar
  40. Rondeau, J.M., Tete-Favier, F., Podjarny, A., Reymann, J.M., Barth, P., Biellman, J.F., & Moras, D. (1992) Novel NADPH-binding domain revealed by the crystal structure of aldose reductase. Nature 355: 469–472PubMedCrossRefGoogle Scholar
  41. Sallaud, C., El Turk, C., Bigerre, L., Sevin, H., Welle, R., & Esnault, R. (1995) Nucleotide sequence of three chalcone reductase genes from alfalfa. Plant Physiology 108: 869–870PubMedCrossRefGoogle Scholar
  42. Samaras, N. & Spithill, T.W. (1989) The developmentally regulated P100/11E gene of Leishmania major shows homology to a superfamily of reductase genes. J. Biol. Chem. 264: 4251–4254PubMedGoogle Scholar
  43. Scott, V.E., Rettig, J., Parcej, D.N., Keen, J.N., Findlay, J.B., Pongs, O., & Dolly, J.O. (1994) Primary structure of a beta-subunit of alpha-dendrotoxin-sensitive K+ channels from bovine brain. Proc. Natl. Acad. Sci. USA 91: 1637–1641PubMedCrossRefGoogle Scholar
  44. Stolz, A., Hammond, L., Lou, H., Takikawa, H., Ronk, M., & Shively, J.E. (1993) cDNA cloning and expression of the human bile-acid binding protein. J. Biol. Chem. 268: 10448–10457PubMedGoogle Scholar
  45. Takahasi, M., Fujii, J., Teshima, T., Suzuki, K., Shiba, T., & Taniguchi, N (1993) Identity of a major 3-deoxyglucosone reducing enzyme with aldehyde reductase in rat liver established by amino acid sequencing and cDNA expression. Gene 127: 249–253CrossRefGoogle Scholar
  46. Tomarev, S.I., Zinovieva, R.D., Dolgilevich, S.M., Luchin, S.V., Krayev, A.S., Skyryabin, K.G., & Gause, G.G. (1984) A novel type of crystallin in the frog eye lens. FEBS Letters 171: 297–301PubMedCrossRefGoogle Scholar
  47. Turner, A.J. and Flynn, T.G. (1982) The nomenclature of aldehyde reductases in Enzymology of Carbonyl Metabolism: Aldehyde Dehydrogenase and Aldo/Keto Reductase (Weiner, H., and Wermuth, B., eds.) pp. 401–402, Alan Liss, New YorkGoogle Scholar
  48. Warren, J.C., Murdock, G.L., Ma, Y., Goodman, S.R., & Zimmer, W.E. (1993) Molecular cloning of testicular 20α-hydroxysteroid dehydrogenase: identity with aldose reductase. Biochemistry 32: 1401–1406PubMedCrossRefGoogle Scholar
  49. Watanabe, K., Fujii, Y., Nakayama, K., Ohkubo, H., Kuramitsu, S., Kagamiyama, H., Nakanishi, S., & Hayaishi, O. (1988) Structural similarity of bovine lung prostaglandin F synthase to lens ε-crystallin of the European common frog. Proc. Natl. Acad. Sci. USA 85: 11–15PubMedCrossRefGoogle Scholar
  50. Welle, R., Schroder, G., Schiltz, E., Grisebach, H., & Schroder, J. (1991) Induced plant responses to pathogen attack Eur. J. Biochem. 196: 423–430PubMedCrossRefGoogle Scholar
  51. Wermuth, B., Omar, A., Forster, A., di Francesco, G., Wolf, M., von Wartbuth, J.P., Bullock, B., & Gabbay, K.H. (1987) Primary structure of aldehyde reductase from human liver. Prog. Clin. Biol. Res. 232: 297–307PubMedGoogle Scholar
  52. Willey, D.L., Caswell, D.A., Lowe, C.R., & Bruce, N.C. (1993) Nucleotide sequence and over-expression of morphine dehydrogenase, a plasmid-encoded gene from Pseudomonas putida M10. Biochem. J. 290: 539–544PubMedGoogle Scholar
  53. Wilson, D.K., Bohren, K.M., Gabbay, K.H., & Quiocho, F.A. (1992) An unlikely sugar substrate site in the 1.65 Å structure of the human aldose reductase holoenzyme implicated in diabetic complications. Science 257: 81–84PubMedCrossRefGoogle Scholar
  54. Wilson, D.K., Nakano, T., Petrash, J.M., & Quiocho, F.A. (1995) 1.7 Å Structure of FR-1, a fibroblast growth factor-induced member of the aldo-keto reductase family, complexed with coenzyme and inhibitor. Biochemistry 34: 14323–14330PubMedCrossRefGoogle Scholar
  55. Winters, C.J., Molowa, D.T., & Guzelian, P.S. (1990) Isolation and characterization of cloned cDNAs encoding human liver chlordecone reductase. Biochemistry 29: 1080–1087PubMedCrossRefGoogle Scholar

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© Springer Science+Business Media New York 1996

Authors and Affiliations

  1. 1.Department of Biochemistry and BiophysicsUniversity of Pennsylvania Medical SchoolPhiladelphiaUSA
  2. 2.Department of BiochemistryQueen’s UniversityCanada
  3. 3.Department of PharmacologyUniversity of Pennsylvania Medical SchoolPhiladelphiaUSA

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