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Structure of porcine aldehyde reductase holoenzyme

Nature Structural Biology volume 2, pages 687–692 (1995)Cite this article

Abstract

Aldehyde reductase, a member of the aldo-keto reductase superfamily, catalyzes the NADPH-dependent reduction of a variety of aldehydes to their corresponding alcohols. The structure of porcine aldehyde reductase–NADPH binary complex has been determined by X-ray diffraction methods and refined to a crystallographic R-factor of 0.20 at 2.4 Å resolution. The tertiary structure of aldehyde reductase is similar to that of aldose reductase and consists of an α/β-barrel with the active site located at the carboxy terminus of the strands of the barrel. Unlike aldose reductase, the Nε2 of the imidazole ring of His 113 in aldehyde reductase interacts, through a hydrogen bond, with the amide group of the nicotinamide ring of NADPH.

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Authors and Affiliations

  1. The University of Alabama at Birmingham, Center for Macromolecular Crystallography, Birmingham, Alabama, 35294-0005, USA

    Ossama El-Kabbani, Ken Judge & Lawrence J. DeLucas

  2. Argonne National Laboratory Structural Biology Center, c/o Brookhaven National Laboratory, Building 725, National Synchrotron Light Source, Beamline X8C, Upton, New York, 11973-5000, USA

    Stephan L. Ginell

  3. Keele University, Physics Department, Keele, Staffordshire, ST5 5BG, UK

    Dean A. A. Myles

  4. Queen's University, Department of Biochemistry, Kingston, Ontario, K7L 3N6, Canada

    T. Geoffrey Flynn

Authors
  1. Ossama El-Kabbani
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  2. Ken Judge
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  4. Dean A. A. Myles
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  5. Lawrence J. DeLucas
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  6. T. Geoffrey Flynn
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El-Kabbani, O., Judge, K., Ginell, S. et al. Structure of porcine aldehyde reductase holoenzyme. Nat Struct Mol Biol 2, 687–692 (1995). https://doi.org/10.1038/nsb0895-687

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