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Aldehyde Reductase

Catalytic Mechanism and Substrate Recognition

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Enzymology and Molecular Biology of Carbonyl Metabolism 6

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

Abstract

Aldehyde reductase is a member of a superfamily of NADPH-dependent aldo-keto reductases, which comprises well over 30 different proteins in seven subfamilies. The enzymes of this superfamily are monomeric proteins with the molecular weight between 30 and 40 kDa. They are characterized by a broad substrate specificity and a great preference of the reduction reaction. They share many common structural and functional characteristics, namely an α/β barrel tertiary structure, a NADPH cofactor which is enfolded by a mobile loop that varies among the different members, and an active site located at the C-terminus of the barrel (Wilson et al., 1992, Harrison et al., 1994, El-Kabbani et al., 1995). The physiological role(s) of these enzymes have not yet been completely established but many are thought to be involved in general detoxification of reactive aldehydes (Bachur, 1976). More specific functions were found for some members, e.g., osmoregulation within the renal tubular cells (aldose reductase; Garcia-Perez and Burg, 1991) or bile acids metabolism (bile acid binders; Stolz et al., 1995). The most studied member of this protein family, aldose reductase, is implicated in the pathogenesis of certain diabetic complications (Gabbay, 1973; Dvornik, 1987; Kador, 1988). Aldehyde and aldose reductase differ significantly in their substrate specificity and tissue distribution (Davidson et al., 1977; Wermuth, 1982), and despite similar kinetic mechanisms, there are differences in the function of the two enzymes that are not yet understood.

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Author information

Authors and Affiliations

  1. Department of Cell Biology, Baylor College of Medicine, Houston, Texas, 77030, USA

    Kenneth H. Gabbay

  2. Department of Pediatrics, Molecular Diabetes and Metabolism Section, Baylor College of Medicine, Houston, Texas, 77030, USA

    Oleg A. Barski & Kurt M. Bohren

Authors
  1. Oleg A. Barski
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  2. Kenneth H. Gabbay
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  3. Kurt M. Bohren
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Editor information

Editors and Affiliations

  1. Purdue University, West Lafayette, Indiana, USA

    Henry Weiner

  2. University of South Dakota School of Medicine, Vermillion, South Dakota, USA

    Ronald Lindahl

  3. Indiana University School of Medicine, Indianapolis, Indiana, USA

    David W. Crabb

  4. Queen’s University, Kingston, Ontario, Canada

    T. Geoffrey Flynn

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© 1996 Springer Science+Business Media New York

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Barski, O.A., Gabbay, K.H., Bohren, K.M. (1996). Aldehyde 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_50

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  • DOI: https://doi.org/10.1007/978-1-4615-5871-2_50

  • 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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