Format

Send to

Choose Destination
See comment in PubMed Commons below
Cell Biochem Biophys. 2003;38(1):79-101.

Structural biology of the aldo-keto reductase family of enzymes: catalysis and cofactor binding.

Author information

  • 1Institute of Molecular Biophysics and Department of Chemistry and Biochemistry, Florida State University, Tallahassee, 32306, USA.

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.

PMID:
12663943
DOI:
10.1385/CBB:38:1:79
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Springer
    Loading ...
    Support Center