A Tryptophan Pyrrole-Ring Cleavage Enzyme in the Most Primitive Eukaryote

  • Y. Iwamoto
  • I. S. Matsui Lee
  • M. Tsubaki
  • R. Kido
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 398)


Two types of dioxygenases that catalyze the oxidative cleavage of the pyrrole ring of tryptophan by insertion of molecular oxygen to yield N-formylkynurenine have been reported (Feigelson and Brady, 1974). One is tryptophan 2,3-dioxygenase (TDO), and the other is indoleamine 2,3-dioxygenase (IDO). Although protoheme IX is a sole prosthetic group for both dioxygenases (Feigelson and Brady, 1974; Hirata and Hayaishi, 1975; Ishimura et al., 1980), these have proved to be distinct enzymes. TDO is a tetrameric protein (M.W. 120,000–167,000) metabolizing L-tryptophan specifically (Feigelson and Brady, 1974). This dioxygenase requires nonspecific reductants such as L-ascorbic acid for its activation in vitro (Feigelson and Brady, 1974). IDO is a monomeric protein (M.W. 41,000) (Shimizu et al., 1978) exhibiting a wide substrate specificity for various indoleamine derivatives including L-and D-tryptophan and serotonin (Ishimura et al., 1970). This enzyme can be also activated by a wide variety of reductants. In addition, methylene blue (or toluidine blue) is absolutely required as an electron mediator from a reductant to the ferric enzyme for its activation (Yamamoto and Hayaishi, 1967).


Methylene Blue Protein Spot Pyrrole Ring Electron Mediator Wide Substrate Specificity 
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Copyright information

© Plenum Press, New York 1996

Authors and Affiliations

  • Y. Iwamoto
    • 1
  • I. S. Matsui Lee
    • 1
  • M. Tsubaki
    • 2
  • R. Kido
    • 1
  1. 1.Department of BiochemistryWakayama Medical CollegeWakayamaJapan
  2. 2.Department of Life ScienceFaculty of Science Himeji Institute of TechnologyHyogoJapan

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