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)

Abstract

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).

Keywords

Cellulose Superoxide Electrophoresis Serotonin Pseudomonas 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Brady, F.O., Monaco, M.E., Forman, H.J., Schutz, G., and Feigelson, P., 1972, On the role of copper in activation of and catalysis by tryptophan-2,3-dioxygenase. 4. Indoleamine 2,3-dioxygenase, purification and some properties. J. Biol. Chem.247: 7915.Google Scholar
  2. Dargie, P.J., Agre, M.C., and Lee, H.C., 1990, Comparison of calcium mobilizing activities of cyclic ADP-ribose and inositol trisphosphate. Cell Regul. 1: 279.Google Scholar
  3. Feigelson, P., Ishimura, Y., and Hayaishi, O., 1965, Studies on the role of hematin in the catalytic mechanism of tryptophan pyrrolase. Biochim. Biophys. Acta96: 283.Google Scholar
  4. Feigelson, P., and Brady, F.O., 1974, in Molecular mechanisms of oxygen activation(Hayaishi, O., ed.) pp.84–133, Academic Press, New YorkGoogle Scholar
  5. Galione, A., 1992, Calcium-induced Ca2+ release and its modulation by cyclic ADP-ribose. Trends Pharmacol. Sci.13: 304.CrossRefGoogle Scholar
  6. Hirata, F., and Hayaishi, O., 1975, Studies on indoleamine 2,3-dioxygenase. 1 Superoxide anion as substrate. J. Biol. Chem.250: 5960.Google Scholar
  7. Ishimura, Y., Nozaki, M., and Hayaishi, O., 1970, The oxygenated form of L-tryptophan 2,3-dioxygenase as reaction intermediate., J. Biol. Chem.245: 3593.Google Scholar
  8. Ishimura, Y., Makino, R., Ueno, R., Sakaguchi, K., Brady, F.O., Feigelson, P., Aisen, P., and Hayaishi, O., 1980, Copper is not essential for the catalytic activity of L-tryptophan 2,3-dioxygenase, J. Biol. Chem.255: 3835.Google Scholar
  9. Knox, W.E., 1955, Tryptophan oxidation. Methods Enzymol. 2: 242.CrossRefGoogle Scholar
  10. Koshiyama, H., Lee, H.C., and Tashjian, A.H., 1991, Novel mechanism of intracellular calcium release in pituitary cells. J. Biol. Chem.266: 16985.Google Scholar
  11. Nokihara, K., Morita, N., and Kuriki, T., 1992, Applications of an automated apparatus for two-dimensional electrophoresis, Model TEP-1, for microsequence analyses of proteins. Electrophoresis13: 701.CrossRefGoogle Scholar
  12. Shall, S., 1985, ADP-ribosylation as a cellular control mechanism, in: ADP-ribosylation of proteins ( Althaus, F.R., Hilz, H., and Shall, S., ed.) pp. 9 – 29, Springer-Verlag, BerlinGoogle Scholar
  13. Shimizu, T., Nomiyama, S., Hirata, F., and Hayaishi, O., 1978, Indoleamine 2,3-dioxygenase, purification and some properties. J. Biol. Chem.253: 4700.Google Scholar
  14. Takasawa, S., Nata, K., Yonekura, H., and Okamoto, H., 1993, Cyclic ADP-ribose in insulin secretion from pancreatic β cells. Science(Washington, D.C.) 259: 370.CrossRefGoogle Scholar
  15. Ueda, K., and Hayaishi, O., 1985, ADP-ribosylation. Annu. Rev. Biochem.54, 73.CrossRefGoogle Scholar
  16. Yamamoto, S., and Hayaishi, O., 1967, Tryptophan pyrrolase of rabbit intestine. J. Biol. Chem.242: 5260.Google Scholar
  17. Yamazaki, F., Kuroiwa, T., Takikawa, O., and Kido, R., 1985, Human indolylamine 2,3-doxygenase, its tissue distribution, and characterization of the placental enzyme. Biochem. J.230: 635.Google Scholar

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

Personalised recommendations