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)


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.


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