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The substrate specificity of tocopherol cyclase

A Stocker1, H Fretz, H Frick

  • 1Organisch-chemisches Institut der Universität Zürich, Switzerland.

Bioorganic & Medicinal Chemistry
|July 1, 1996
PubMed
Summary
This summary is machine-generated.

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Tocopherol cyclase from Anabaena variabilis recognizes substrates via hydroxyl group, double bond configuration, and side chain length. Hydrophobic tails likely guide substrates to the enzyme active site.

Area of Science:

  • Biochemistry
  • Enzymology
  • Cyanobacteria research

Background:

  • Tocopherol cyclase is crucial for tocopherol biosynthesis.
  • Understanding enzyme-substrate interactions is key to metabolic pathway elucidation.

Purpose of the Study:

  • To investigate the substrate specificity of Anabaena variabilis tocopherol cyclase.
  • To identify key structural features of substrates recognized by the enzyme.

Main Methods:

  • Enzyme assays using 11 substrate analogues.
  • Affinity chromatography with two matrices.

Main Results:

  • The enzyme specifically recognizes the C(1) hydroxyl group of the hydroquinone.
  • The (E)-configuration of the double bond is critical for substrate binding.

Related Experiment Videos

  • The length of the lipophilic side chain significantly influences substrate recognition.
  • Affinity matrix experiments indicate hydrophobic tail-driven substrate approach.

    • Conclusions:

    • Anabaena variabilis tocopherol cyclase exhibits distinct substrate recognition sites.
    • The enzyme's active site accommodates substrates through specific interactions with the hydroquinone head and hydrophobic tail orientation.