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

Abstract

The aldo-keto reductase superfamily (Bohren et al., 1989) consists of many reductases that differ in their primary structure, substrate specficities and catalytic properties. Many subfamilies have been recognized, including the aldose reductase, aldehyde reductase, 3α-hydroxysteroid dehydrogenase, androgen regulated protein from the mouse vas deferens, and many more. In the course of cloning murine liver aldo-keto reductases, we discovered yet another aldo-keto reductase with some unique properties. We hereby describe the cloning, sequencing, over-expression and characterization of this novel murine aldo-keto reductase which appears to be uniquely different from any hitherto described member of the superfamily.

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References

  • Bohren KM, Bullock B, Wermuth B, Gabbay KH. (1989) Aldo-keto reductase superfamily: cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J Biol Chem 264:9547–9551.

    PubMed  CAS  Google Scholar 

  • Bohren KM, Page JL, Shankar R, Henry SP, and Gabbay KH (1991) Expression of Human Aldose and Aldehyde Reductases: Site-directed Mutagenesis of a Critical Lysine-262. J. Biol. Chem. 266:24031–24037.

    PubMed  CAS  Google Scholar 

  • Bohren KM, Grimshaw CE, Lai C-J, Harrison DH, Ringe D, Petsko GA, Gabbay KH. (1994) Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and the crystal structure of the Y48H mutant enzyme. Biochemistry 33:2021–2032.

    Article  PubMed  CAS  Google Scholar 

  • Bruce NC, Willey DL, Coulson AFW, Jeffery J. (1994) Bacterial morphine dehydrogenase further defines a distinct superfamily of oxidoreductases with diverse functional activities. Biochemistry 299:805–811.

    CAS  Google Scholar 

  • Cheng K-C, White PC, and Qin K-N (1991) Molecular Cloning and Expression of Rat LiveT 3α-hydroxysteroid dehydrogenase. Mol. Endocrinol. 5, 823–828.

    Article  PubMed  CAS  Google Scholar 

  • Dayhoff, MO, Schwartz, RM, and Orcutt, BC (1978) in Atlas of Protein Sequence and Structure (Dayhoff, MO ed) Vol 5 Suppl. 3 pp 345–352, National Biomedical Research Foundation, Washington, D.C.

    Google Scholar 

  • Donohue, PJ, Alberts, GF, Hampton BS, and Winkles JA (1994) A delayed-early Gene activated by fibroblast growth factor-1 encodes a protein related to aldose reductase, J. Biol.Chem. 269, 8604–8609.

    PubMed  CAS  Google Scholar 

  • Ehrig T, Bohren KM, Prendergast F G, and Gabbay KH (1994) Mechanism of aldose reductase inhibition: Binding of NADP+/NADPH and alrestatin-like inhibitors, Biochemistry 33, 7157–7165.

    Article  PubMed  CAS  Google Scholar 

  • GCG, Genetics Computer Group, Program Manual for the Wisconsin Package, Version 8, September 1994, 575 Science Drive, Madison, Wisconsin, USA 53711.

    Google Scholar 

  • Grimshaw CE, Shahbaz M, and Putney CG. (1990) Mechanistic basis fo nonlinear kinetics of aldehyde reduction catalyzed by aldose reductase. Biochemistry 29:9947–9955.

    Article  PubMed  CAS  Google Scholar 

  • Grimshaw CE, Bohren KM, Lai C-J, and Gabbay KH (1995). Human aldose reductase: Rate constants for a mechanism including interconversion of ternary complexes by recombinant wild type enzyme. Biochemistry 34, 14356–14365.

    Article  PubMed  CAS  Google Scholar 

  • Grimshaw CE, Bohren KM, Lai C-J, and Gabbay KH (1995). Human Aldose Reductase: Subtle Effects Revealed by Rapid Kinetic Studies of the C298A Mutant Enzyme. Biochemistry 34, 14366–14373.

    Article  PubMed  CAS  Google Scholar 

  • Gui T, Tanimoto T, kokai Y, and Nishimura C (1995) Presence of a closely related subgroup in the aldo-keto reductase family of the mouse. Eur. J. Biochem. 227., 448–453.

    Article  PubMed  CAS  Google Scholar 

  • Kubiseski TJ, Hyndman DJ, Morjana NA, and Flynn TG. (1992) Studies on pig muscle aldose reductase. J Biol Chem 267:6510–6517.

    PubMed  CAS  Google Scholar 

  • Kubiseski TJ and Flynn TG (1995) Studies on human aldose reductase. Probing the role of arginine 268 by site-directed mutagenesis. J. Biol. Chem 270, 16911–16917.

    Article  PubMed  CAS  Google Scholar 

  • Pailhoux EA, Martinez, A., Veyssiere GM, Jean CG. (1990) cDNA cloning and protein homology with aldo-keto reductase superfamily. J. Biol. Chem. 256:19932–19936.

    Google Scholar 

  • Varma, SD., and Kinoshita, JH. (1974) The absence of cataracts in mice with congenital hyperglycemia, Exp.Eye. Res. 19, 577–582.

    Article  PubMed  CAS  Google Scholar 

  • Varma SD, Mizuno F, Kinoshita JH (1977) Diabetic Cataracts and Flavonoids. Science 195, 205–206.

    Article  PubMed  CAS  Google Scholar 

  • Watanabe, K., Fujii, Y., Nakayama, K Ohkubo, H., Kuramitsu, S Kagamiyama, H., Nakanishi, S and Hayaishi, O (1988) Structural similarity of bovine lung prostaglandin F synthase to lens s-crystallin of the Proc.Natl. Acad.Sci. U.S.A. 85, 11–15.

    Article  CAS  Google Scholar 

  • Wilson DK, Bohren KM, Gabbay KH, Quiocho FA. (1992) An unlikely sugar substrate site in the 1.65 Å structure of human aldose reductase holoenzyme implicated in diabetic complications. Science 257:81–84.

    Article  PubMed  CAS  Google Scholar 

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© 1996 Springer Science+Business Media New York

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Bohren, K.M., Barski, O.A., Gabbay, K.H. (1996). Characterization of a Novel Murine Aldo-Keto Reductase. In: Weiner, H., Lindahl, R., Crabb, D.W., Flynn, T.G. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 6. Advances in Experimental Medicine and Biology, vol 414. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5871-2_52

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  • DOI: https://doi.org/10.1007/978-1-4615-5871-2_52

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-7692-7

  • Online ISBN: 978-1-4615-5871-2

  • eBook Packages: Springer Book Archive

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