Skip to main content
SpringerLink
Log in

Indoleamine-pyrrole 2,3-dioxygenase

  • Chapter
Springer Handbook of Enzymes

Part of the book series: Springer Handbook of Enzymes ((HDBKENZYMES,volume 25))

  • 65 Accesses

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 259.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 329.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 329.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Badawy, A.A.: Central role of tryptophan pyrrolase in haem metabolism. Biochem. Soc. Trans., 7, 575–583 (1979)

    PubMed  CAS  Google Scholar 

  2. Feigelson, P.; Brady, F.O.: Heme-containing dioxygenases. Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York, 87–133 (1974)

    Google Scholar 

  3. Maezono, K.; Tashiro, K.; Nakamura, T.: Deduced primary structure of rat tryptophan-2,3-dioxygenase. Biochem. Biophys. Res. Commun., 170, 176–181 (1990)

    Article  PubMed  CAS  Google Scholar 

  4. Hitchcock, M.J.M.; Katz, E.: Purification and characterization of tryptophan dioxygenase from Streptomyces parvulus. Arch. Biochem. Biophys., 261, 148–160 (1988)

    Article  PubMed  CAS  Google Scholar 

  5. Matsumura, M.; Osada, K.; Aiba, S.: l-Tryptophan 2,3-dioxygenase of a moderate thermophile, Bacillus brevis. Purification, properties and a substrate-mediated stabilization of the quaternary structure. Biochim. Biophys. Acta, 786, 9–17 (1984)

    PubMed  CAS  Google Scholar 

  6. Uchida, K.; Shimizu, T.; Makino, R.; Sakaguchi, K.; Iizuka, T.; Ishimura, Y.: Magnetic and natural circular dichroism of l-tryptophan 2,3-dioxygenases and indoleamine 2,3-dioxygenase. I. Spectra of ferric and ferrous high spin forms. J. Biol. Chem., 258, 2519–2525 (1983)

    PubMed  CAS  Google Scholar 

  7. Sono, M.: Spectroscopic and equilibrium studies of ligand and organic substrate binding to indolamine 2,3-dioxygenase. Biochemistry, 29, 1451–1460 (1990)

    Article  PubMed  CAS  Google Scholar 

  8. Sono, M.: The roles of superoxide anion and methylene blue in the reductive activation of indoleamine 2,3-dioxygenase by ascorbic acid or by xanthine oxidase-hypoxanthine. J. Biol. Chem., 264, 1616–1622 (1989)

    PubMed  CAS  Google Scholar 

  9. Yoshida, R.; Hayaishi, O.: Indoleamine 2,3-dioxygenase. Methods Enzymol., 142, 188–195 (1987)

    PubMed  CAS  Google Scholar 

  10. Sono, M.; Dawson, J.H.: Extensive studies of the heme coordination structure of indoleamine 2,3-dioxygenase and of tryptophan binding with magnetic and natural circular dichroism and electron paramagnetic resonance spectroscopy. Biochim. Biophys. Acta, 789, 170–187 (1984)

    PubMed  CAS  Google Scholar 

  11. Yoshida, R.; Hayaishi, O.: Overview: superoxygenase. Methods Enzymol., 105, 61–70 (1984)

    PubMed  CAS  Google Scholar 

  12. Shimizu, T.; Nomiyama, S.; Hirata, E; Hayaishi, O.: Indoleamine 2,3-dioxygenase. Purification and some properties. J. Biol. Chem., 253, 4700–4706 (1978)

    PubMed  CAS  Google Scholar 

  13. Littlejohn, T.K.; Takikawa, O.; Skylas, D.; Jamie, J.E; Walker, M.J.; Truscott, R.J.W.: Expression and purification of recombinant human indoleamine 2,3-dioxygenase. Protein Expr. Purif., 19, 22–29 (2000)

    Article  PubMed  CAS  Google Scholar 

  14. Salter, M.; Hazelwood, R.; Pogson, C.I.; Iyer, R.; Madge, D.J.: The effects of a novel and selective inhibitor of tryptophan 2,3-dioxygenase on tryptophan and serotonin metabolism in the rat. Biochem. Pharmacol., 49, 1435–1442 (1995)

    Article  PubMed  CAS  Google Scholar 

  15. Thomas, S.R.; Mohr, D.; Stocker, R.: Nitric oxide inhibits indoleamine 2,3-dioxygenase activity in interferon-γ primed mononuclear phagocytes. J. Biol. Chem., 269, 14457–14464 (1994)

    PubMed  CAS  Google Scholar 

  16. Dang, Y.; Dale, W.E.; Brown, O.R.: Comparative effects of oxygen on indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase of the kynurenine pathway. Free Radic. Biol. Med., 28, 615–624 (2000)

    Article  PubMed  CAS  Google Scholar 

  17. Friberg, M.; Jennings, R.; Alsarraj, M.; Dessureault, S.; Cantor, A.; Extermann, M.; Mellor, A.L.; Munn, D.H.; Antonia, S.J.: Indoleamine 2,3-dioxygenase contributes to tumor cell evasion of T cell-mediated rejection. Int. J. Cancer, 101, 151–155 (2002)

    Article  PubMed  CAS  Google Scholar 

  18. Hissong, B.D.; Byrne, G.I.; Padilla, M.L.; Carlin, J.M.: Upregulation of interferon-induced indoleamine 2,3-dioxygenase in human macrophage cultures by lipopolysaccharide, muramyl tripeptide, and interleukin-1. Cell. Immunol., 160, 264–269 (1995)

    Article  PubMed  CAS  Google Scholar 

  19. Takikawa, O.; Littlejohn, T.K.; Truscott, R.J.W.: Indoleamine 2,3-dioxygenase in the human lens, the first enzyme in the synthesis of UV filters. Exp. Eye Res., 72, 271–277 (2001)

    Article  PubMed  CAS  Google Scholar 

  20. Dick, R.; Murray, B.P.; Reid, M.J.; Correia, M.A.: Structure-function relationships of rat hepatic tryptophan 2,3-dioxygenase: Identification of the putative heme-ligating histidine residues. Arch. Biochem. Biophys., 392, 71–78 (2001)

    Article  PubMed  CAS  Google Scholar 

  21. Kudo, Y.; Boyd, C.A.R.; Sargent, I.L.; Redman, C.W.G.: Tryptophan degradation by human placental indoleamine 2,3-dioxygenase regulates lymphocyte proliferation. J. Physiol., 535, 207–215 (2001)

    Article  PubMed  CAS  Google Scholar 

  22. Kudo, Y.; Boyd, C.A.R.: Human placental indoleamine 2,3-dioxygenase: cellular localization and characterization of an enzyme preventing fetal rejection. Biochim. Biophys. Acta, 1500, 119–124 (2000)

    PubMed  CAS  Google Scholar 

  23. Musso, T.; Gusella, G.L.; Brooks, A.; Longo, D.L.; Varesio, L.: Interleukin-4 inhibits indoleamine 2,3-dioxygenase expression in human monocytes. Blood, 83, 1408–1411 (1994)

    PubMed  CAS  Google Scholar 

  24. Frumento, G.; Rotondo, R.; Tonetti, M.; Damonte, G.; Benatti, U.; Ferrara, G.B.: Tryptophan-derived catabolites are responsible for inhibition of T and natural killer cell proliferation induced by indoleamine 2,3-dioxygenase. J. Exp. Med., 196, 459–468 (2002)

    Article  PubMed  CAS  Google Scholar 

  25. Terentis, A.C.; Thomas, S.R.; Takikawa, O.; Littlejohn, T.K.; Truscott, R.J.W.; Armstrong, R.S.; Yeh, S.R.; Stocker, R.: The heine environment of recombinant human indoleamine 2,3-dioxygenase: Structural properties and substrate-ligand interactions. J. Biol. Chem., 277, 15788–15794 (2002)

    Article  PubMed  CAS  Google Scholar 

  26. Stowell, L.; Morland, J.: The influence of some methodological factors on measurement of tryptophan oxygenase activities in crude homogenates of rat liver. Biochem. J., 209, 831–836 (1983)

    PubMed  CAS  Google Scholar 

  27. Schmid, W.; Scherer, G.; Danesch, U.; Zentgraf, H.; Matthias, E; Strange, C.M.; Roewekamp, W.; Schuetz, G.: Isolation and characterization of the rat tryptophan oxygenase gene. EMBO J., 1, 1287–1293 (1982)

    PubMed  CAS  Google Scholar 

  28. Ishimura, Y.; Makino, R.; Iizuka, T.: Regulatory control and catalytic mechanisms of l-tryptophan 2,3-dioxygenase (pyrrolase). Adv. Enzyme Regul., 18, 291–302 (1980)

    Article  PubMed  CAS  Google Scholar 

  29. Rouach, H.; Ribiere, C.; Nordmann, J.; Nordmann, R.: In vitro inhibition of rat liver tryptophan oxygenase by 4-hydroxypyrazole. FEBS Lett., 101, 149–152 (1979)

    Article  PubMed  CAS  Google Scholar 

  30. Hayaishi, O.: Properties and function of indoleamine 2,3-dioxygenase. J. Biochem., 79, 13p–21p (1976)

    Google Scholar 

  31. Ren, S.; Liu, H.; Licad, E.; Correia, M.A.: Expression of rat liver tryptophan 2,3-dioxygenase in Escherichia coli: structural and functional characterization of the purified enzyme. Arch. Biochem. Biophys., 333, 96–102 (1996)

    Article  PubMed  CAS  Google Scholar 

  32. Schartau, W.; Linzen, B.: The tryptophan 2,3-dioxygenase of the blowfly, Protophormia terrae-novae: partial purification and characterization. Hoppe-Seyler’s Z. Physiol. Chem., 357, 41–49 (1976)

    PubMed  CAS  Google Scholar 

  33. Chen, J.; Matchett, W.H.: Occurrence of N-formylkynurenine in extracts of Neurospora crassa: evidence for the activity of tryptophan pyrrolase. J. Bacteriol., 118, 837–843 (1974)

    PubMed  CAS  Google Scholar 

  34. Brady, F.O.; Feigelson, P.: Photoactivation of pseudomonad l-tryptophan oxygenase by electron ejection from its substrate, l-tryptophan. Arch. Biochem. Biophys., 156, 745–750 (1973)

    Article  PubMed  CAS  Google Scholar 

  35. Diamond, E.M.; Jedeikin, A.; Kench, J.E.: Purification of tryptophan oxygenase and its interaction with cadmium. Biochem. Biophys. Res. Commun., 52, 679–686 (1973)

    Article  PubMed  CAS  Google Scholar 

  36. Schutz, G.; Feigelson, P.: Purification and properties of rat liver tryptophan oxygenase. J. Biol. Chem., 247, 5327–5332 (1972)

    PubMed  CAS  Google Scholar 

  37. Brady, F.O.; Monaco, M.E.; Forman, H.J.; Schutz, G.; Feigelson, P.: On the role of copper in activation of and catalysis by tryptophan-2,3-dioxygenase. J. Biol. Chem., 247, 7915–7922 (1972)

    PubMed  CAS  Google Scholar 

  38. Knox, W.E.; Yip, A.; Reshef, L.: l-Tryptophan 2,3-dioxygenase (tryptophan pyrrolase) (rat liver). Methods Enzymol., 17A, 415–421 (1970)

    Article  Google Scholar 

  39. Schimke, R.T.: l-Tryptophan 2,3-dioxygenase (tryptophan pyrrolase) (rat liver). Methods Enzymol., 17A, 421–428 (1970)

    Google Scholar 

  40. Ishimura, Y.: l-Tryptophan 2,3-dioxygenase (tryptophan pyrrolase) (Pseudomonas fluorescens). Methods Enzymol., 17A, 429–434 (1970)

    Article  Google Scholar 

  41. Yamamoto, S.; Hayaishi, O.: Tryptophan 2,3-dioxygenase (tryptophan pyrrolase) (rabbit intestine). Methods Enzymol., 17A, 434–438 (1970)

    Google Scholar 

  42. Poillon, W.N.; Maeno, H.; Koike, K.; Feigelson, P.: Tryptophan oxygenase of Pseudomonas acidovorans. Purification, composition, and subunit structure. J. Biol. Chem., 244, 3447–3456 (1969)

    PubMed  CAS  Google Scholar 

  43. Brown, J.N.; Dodgen, C.L.: Fish liver tryptophan pyrrolase: the apparent absence of both hormonal regulation and substrate induction. Biochim. Biophys. Acta, 165, 463–469 (1968)

    CAS  Google Scholar 

  44. Paik, W.K.; Christinzio, M.; Kim, S.: Liver tryptophan pyrrolase activity during thyrosine-induced metamorphosis of Rana catesbeiana. Biochim. Biophys. Acta, 167, 209–212 (1968)

    PubMed  CAS  Google Scholar 

  45. Ishiguro, I.; Naito, J.; Saito, K.; Nagamura, Y.: Skin l-tryptophan-2,3-dioxygenase and rat hair growth. FEBS Lett., 329, 178–182 (1993)

    Article  PubMed  CAS  Google Scholar 

  46. Terness, P.; Bauer, T.M.; Rose, L.; Dufter, C.; Watzlik, A.; Simon, H.; Opelz, G.: Inhibition of allogeneic T cell proliferation by indoleamine 2,3-dioxygenase-expressing dendritic cells: mediation of suppression by tryptophan metabolites. J. Exp. Med., 196, 447–457 (2002)

    Article  PubMed  CAS  Google Scholar 

  47. Daya, S.; Anoopkumar-Dukie, S.: Acetaminophen inhibits liver trytophan-2,3-dioxygenase activity with a concomitant rise in brain serotonin levels and a reduction in urinary 5-hydroxyindole acetic acid. Life Sci., 67, 235–240 (2000)

    Article  PubMed  CAS  Google Scholar 

  48. Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gas-teiger, E.; Martin M.J.; Michoud, K.; O’Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.: The SWISS-PROT protein knowledgebase and its supplement TrEMBL. Nucleic Acids Res., 31, 365–370 (2003)

    Article  PubMed  CAS  Google Scholar 

  49. Comings, D.E.; Muhleman, D.; Dietz, G.; Sherman, M.; Forest, G.L.: Sequence of human tryptophan 2,3-dioxygenase (TDO2): presence of a glucocorticoid response-like element composed of a GTT repeat and an intronic CCCCT repeat. Genomics, 29, 390–396 (1995)

    Article  PubMed  CAS  Google Scholar 

  50. Serles, L.L.; Ruth, R.S.; Pret, A.M.; Fridell, R.A.; Ali, A.J.: Structure and transcription of the Drosophila melanogaster vermillion gene and several mutant alleles. Mol. Cell. Biol., 10, 1423–1431 (1990)

    Google Scholar 

  51. Habara-Ohkubo, A.; Takikawa, O.; Yoshida, R.: Cloning and expression of a cDNA encoding mouse indoleamine 2,3-dioxygenase. Gene, 105, 221–227 (1991)

    Article  PubMed  CAS  Google Scholar 

  52. Kadoya, A.; Tone, S.; Mareda, H.; Minatogawa, Y.; Kido, R.: Gene structure of human indoleamine 2,3-dioxygenase. Biochem. Biophys. Res. Commun., 189, 530–536 (1992)

    Article  PubMed  CAS  Google Scholar 

  53. Dai, W.; Gupta, S.L.: Molecular cloning, sequencing and expression of human interferon-γ-inducible indoleamine 2,3-dioxygenase cDNA. Biochem. Biophys. Res. Commun., 168, 1–8 (1990)

    Article  PubMed  CAS  Google Scholar 

  54. Tone, S.; Takikawa, O.; Habara-Ohkubo, A.; Kadoxa, A.; Yoshida, R.; Kido, R.: Primary structure of human indoleamine 2,3-dioxygenase deduced from the nucleotide sequence of its cDNA. Nucleic Acids Res., 18, 367 (1990)

    Article  PubMed  CAS  Google Scholar 

Download references

Editor information

Editors and Affiliations

  1. Institute for Biochemistry, University to Cologne, Zülpicher Strasse 47, 50674, Cologne, Germany

    Dietmar Schomburg  & Ida Schomburg  & 

Rights and permissions

Reprints and permissions

Copyright information

© 2006 Springer-Verlag Berlin Heidelberg

About this chapter

Cite this chapter

(2006). Indoleamine-pyrrole 2,3-dioxygenase. In: Schomburg, D., Schomburg, I. (eds) Springer Handbook of Enzymes. Springer Handbook of Enzymes, vol 25. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-37704-2_88

Download citation

Publish with us

Policies and ethics

Search

Navigation