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Is Indoleamine 2,3-Dioxygenase Another Heme and Copper Containing Enzyme?

  • Frank O. Brady
  • Albert Udom
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 74)

Abstract

Indoleamine 2,3-dioxygenase catalyzes a reaction similar to that catalyzed by L-tryptophan 2,3-dioxygenases except that the former shows little substrate specificity while the latter shows absolute specificity for L-tryptophan. Originally referred to as D-tryptophan oxygenase, indoleamine 2,3-dioxygenase has been detected in and/or purified from rabbit small intestine (1–7), rabbit brain (8), rat intestine (9), and rat brain (10–11). Serotonin, melatonin, D- and L-5-hydroxytryptophan, tryptamine, and D- and L-tryptophan have been shown to be substrates for indoleamine 2,3-dioxygenase. An unusual characteristic of this enzyme is the requirement for methylene blue and ascorbate in eliciting catalytic activity in vitro (1,2,5), although a recent report suggests that tetrahydrobiopterin can also serve in this process(12). Hirata and Hayaishi (3,5) have implicated the involvement of O 2 - in the reaction catalyzed by indoleamine 2,3-dioxygenase, based mainly on the ability of superoxide dismutase to inhibit the ongoing reaction. Based on my previous work with L-tryptophan 2,3-dioxygenases (13, 14), we became interested in the possibility that indoleamine 2,3-dioxygenase might also be a heme and copper containing enzyme.

Keywords

Methylene Blue Copper Content Atomic Absorption Spectroscopy Visible Absorption Spectrum Rabbit Brain 
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

  • Frank O. Brady
    • 1
  • Albert Udom
    • 1
  1. 1.Department of Biochemistry, School of MedicineThe University of South DakotaVermillionUSA

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