Cell Biochemistry and Biophysics

, Volume 38, Issue 1, pp 79–101 | Cite as

Structural biology of the aldo-keto reductase family of enzymes

Catalysis and cofactor binding
Review Article

Abstract

The aldo-keto reductases (AKR) comprise a large family of oxidoreductases with importance to both health and industrial applications. The redox chemistry of the AKRs is dependent on NAD(P)H as a cofactor. Despite a wealth of structural and biochemical data relating to the interaction of AKRs with specific inhibitors, much less is known regarding the interactions with cofactor or substrate. In particular, while many X-ray structures are available for AKR/inhibitor complexes, they are only a few examples where apo- and holo-forms can be directly compared. Thus, while the role of the cofactor in the redox chemistry is generally understood, the details of the structural dynamics associated with cofactor binding are less clear. Likewise, the structural details of both cofactor and substrate specificity are limited. In this review, we focus on details of the structural biology and molecular dynamics associated with catalysis, cofactor, and substrate binding as elucidated for those AKRs for which apo- and holo-structures are available. Understanding such dynamics may identify a new direction in the design of specific inhibitors.

Index Entries

Aldo-keto reductase structural biology diabetes vitamin C structural dynamics 

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Copyright information

© Humana Press Inc 2003

Authors and Affiliations

  • Gulsah Sanli
    • 1
  • Jocelyn I. Dudley
    • 1
  • Michael Blaber
    • 1
  1. 1.Institute of Molecular Biophysics and Department of Chemistry and BiochemistryFlorida State UniversityTallahassee

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