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Related Experiment Videos

Identifying and manipulating structural determinates linking catalytic specificities in terpene synthases.

Bryan T Greenhagen1, Paul E O'Maille, Joseph P Noel

  • 1Plant Biology Program, Department of Plant and Soil Sciences, University of Kentucky, Lexington, KY 40546-0312, USA.

Proceedings of the National Academy of Sciences of the United States of America
|June 21, 2006
PubMed
Summary

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Researchers interconverted terpene synthase (TPS) functions by altering active site residues. This study reveals how structural changes in TPS enzymes dictate their catalytic specificities and uncovers ancestral biosynthetic activities.

Area of Science:

  • Enzymology
  • Biochemistry
  • Structural Biology

Background:

  • Terpene synthases (TPS) are crucial enzymes producing diverse compounds.
  • TPS enzymes share a conserved structure but exhibit varied specificities.
  • Active site contours, not reactive residues, primarily determine TPS catalytic function.

Purpose of the Study:

  • To investigate the relationship between TPS structure and catalytic specificity.
  • To demonstrate the interconversion of TPS functions through targeted mutagenesis.
  • To identify key residues responsible for differentiating biosynthetic properties.

Main Methods:

  • Comparative analysis of evolutionarily related TPS active sites.
  • Site-directed mutagenesis to replace variable residues within and around the active site.

Related Experiment Videos

  • Biochemical assays to assess enzyme activity and product profiles.

    • Main Results:

    • Reciprocal interconversion of catalytic specificities between two distinct TPS enzymes was achieved.
    • Identification of specific variable residues critical for altering TPS function.
    • Discovery of previously unknown biosynthetic activities suggesting ancestral enzyme capabilities.

    Conclusions:

    • TPS catalytic specificity can be modulated by altering active site residues.
    • This work provides a method for mapping structure-function relationships in TPS.
    • The findings offer a strategy for uncovering ancestral enzyme functions and evolutionary pathways.