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On the Prosthetic Groups of L-Tryptophan 2,3-Dioxygenase from Pseudomonas: Evidence for Noninvolvement of Copper in the Reaction

  • Yuzuru Ishimura
  • Osamu Hayaishi
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 74)

Summary

The amounts of copper present in highly purified preparations of L-tryptophan 2,3-dioxygenase from Pseudomonas fluorescens have been shown to be negligible by six different methods of copper determination. It has also been demonstrated that, during the purification, the heme content of enzyme preparations increased in parallel with the specific enzyme activity, whereas that of copper decreased.

These results, together with the finding that the inhibitory effects of copper chelators on the enzyme could be attributable to some other action of these chemicals rather than to their chelating properties, indicate that copper is not an essential component of L-tryptophan 2,3-dioxygenase.

Keywords

Enzyme Preparation Copper Content Pseudomonas Fluorescens Specific Enzyme Activity Standard Assay Condition 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • Yuzuru Ishimura
    • 1
    • 2
  • Osamu Hayaishi
    • 1
    • 2
  1. 1.Department of Biochemistry, School of MedicineKeio UniversityShinjuku-ku, Tokyo 160Japan
  2. 2.Department of Medical Chemistry, Faculty of MedicineKyoto UniversitySakyo-ku, Kyoto 606Japan

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