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    Acta Crystallogr D Biol Crystallogr. 1994 Nov 1;50(Pt 6):859-68.

    Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications.

    El-Kabbani O, Green NC, Lin G, Carson M, Narayana SV, Moore KM, Flynn TG, DeLucas LJ.

    Source

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

    Abstract

    The crystal structures of porcine and human aldehyde reductase, an enzyme implicated in complications of diabetes, have been determined by X-ray diffraction methods. The crystallographic R factor for the refined porcine aldehyde reductase model is 0.19 at 2.8 A resolution. There are two molecules in the asymmetric unit related by a local non-crystallographic twofold axis. The human aldehyde reductase model has been refined to an R factor of 0.21 at 2.48 A resolution. The amino-acid sequence of porcine aldehyde reductase revealed a remarkable homology with human aldehyde reductase. The coenzyme-binding site residues are conserved and adopt similar conformations in human and porcine aldehyde reductase apo-enzymes. The tertiary structures of aldhyde reductase and aldose reductase are similar and consist of a beta/alpha-barrel, with the coenzyme-binding site located at the carboxy-terminus end of the strands of the barrel. The crystal structure of porcine and human aldehyde reductase should allow in vitro mutagenesis to elucidate the mechanism of action for this enzyme and facilitate the effective design of specific inhibitors.

    PMID:
    15299353
    [PubMed]

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      Cited by 2 PubMed Central articles

      Structures reported by this article

      • Structure molecule image Aldehyde Reductase
        PDB: 2ALR
        Source: Homo sapiens
        Method: X-Ray Diffraction
        Resolution: 2.48 Å

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