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Related Experiment Videos

Sequence and structure of epoxide hydrolases: a systematic analysis.

Sandra Barth1, Markus Fischer, Rolf D Schmid

  • 1Institute of Technical Biochemistry, University of Stuttgart, Germany.

Proteins
|May 18, 2004
PubMed
Summary

Epoxide hydrolases (EHs) are enzymes that break down epoxides. This study classifies EHs into superfamilies and analyzes their structure, revealing conserved regions and key loops for modeling.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Epoxide hydrolases (EHs) are crucial enzymes catalyzing epoxide hydrolysis to vicinal diols.
  • Over 100 EHs are known, but sequence similarity is low, complicating classification.
  • Understanding EH structure and function is vital due to their diverse roles.

Purpose of the Study:

  • To identify conserved regions and analyze the modular architecture of epoxide hydrolases.
  • To classify EHs into homologous families and major superfamilies.
  • To develop a modeling approach for EH structures based on conserved elements.

Main Methods:

  • Multisequence alignment and phylogenetic analysis of 95 EHs.
  • Structural comparison of three known EH structures.

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  • Classification of EHs into three clusters based on loop length variations.

    • Main Results:

    • EHs were grouped into 12 homologous families and 2 superfamilies: microsomal and cytosolic.
    • Structural analysis revealed conserved core and cap domains, with variations in two key loops (NC-loop and cap-loop).
    • A classification system based on loop length enabled modeling of core, cap, NC-loop, and cap-loop regions for a high percentage of EHs.

    Conclusions:

    • The modular architecture of EHs is conserved, with specific loops driving structural diversity.
    • The developed classification and modeling approach facilitate the study of a wide range of EHs.
    • Models of EHs are accessible via the Lipase Engineering Database, aiding further research.