Tryptophan 2,3-dioxygenase: a review of the roles of the heme and copper cofactors in catalysis.

@article{Brady1975Tryptophan2A,
  title={Tryptophan 2,3-dioxygenase: a review of the roles of the heme and copper cofactors in catalysis.},
  author={Frank O. Brady},
  journal={Bioinorganic chemistry},
  year={1975},
  volume={5 2},
  pages={
          167-82
        }
}
  • F. O. Brady
  • Published 1975
  • Biology, Chemistry
  • Bioinorganic chemistry
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10 Citations
Highly Influential Citations
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Background Citations
4

10 Citations

Biochemical and Spectroscopic Characterization of Tryptophan Oxygenation: Tryptophan 2, 3-Dioxygenase and Maug

  • R. Fu
  • Chemistry, Biology
  • 2009
Two unidentified enzymatic activities of ferric TDO from Ralstonia metallidurans are revealed, which are peroxide driven oxygenation and catalase-like activity and stoichiometric titration suggests that two moles of H2O2 were required for the production of one mole of N-formylkynurenine.

Oxygenation of indoles by a copper(I) chloride pyridine complex. A new tryptophan 2,3-dioxygenase model system.

A short history of heme dioxygenases: rise, fall and rise again

  • E. Raven
  • Biology
    JBIC Journal of Biological Inorganic Chemistry
  • 2016
A short history of the early TDO and IDO literature, the people that were involved in creating it, and the legacy that this left for the future are presented.

ESR of Copper in Biological Systems

It is now beyond dispute that small amounts of certain copper proteins play important roles in both animal and plant physiology and that the highest concentrations of copper, in decreasing order, are found in liver, brain, heart, muscle, and kidney.

Macrophages and Iron Metabolism.

Modulating the immune system by amino acid depletion : IDO and beyond

This study investigated the IDO inhibitory properties and mechanism of action of the tryptophan metabolite 3-HAA that potentially forms a negative feedback loop in the kynurenine pathway, and examined mechanisms of T-cell suppression employed by myeloid derived suppressor cells (MDSCs), focusing on their ability to deplete amino acids from their microenvironment.

IDO Induces Expression of a Novel Tryptophan Transporter in Mouse and Human Tumor Cells

It is demonstrated that IDO+ tumor cells express a novel amino acid transporter, which accounts for ∼50% of the tryptophan uptake, and could be a way of pharmacological inhibition of IDO-mediated tumor escape.

Human Tumor Cells Tryptophan Transporter in Mouse and IDO Induces Expression of a Novel

The results indicate that IDO expression, both in mouse and in human tumor cells, results in modified tryptophan uptake through a novel transport system that has functional properties different from those of System L.

Reaction of indoles with molecular oxygen catalyzed by metalloporphyrins

Tryptophan and the immune response

The issue of immunomodulatory actions of tryptophan catabolites is examined in detail, and the possible involvement of quinolinate as a means of replenishing NAD + in leucocytes, which is depleted by oxidative stress during an immune response.

References

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The oxygenated form of L-tryptophan 2,3-dioxygenase as reaction intermediate.

Noninvolvement of copper in the L-tryptophan 2,3-digoxygenase reaction.

The oxygenated complexes of the two catalytically active oxidation-reduction states of L-tryptophan-2,3-dioxygenase.

On the role of copper in activation of and catalysis by tryptophan-2,3-dioxygenase.

It is established that copper, as well as heme, is essential for the catalytic activity of both hepatic and bacterial tryptophan oxygenases and that as the enzyme develops a requirement for an exogenous reductant, such as ascorbate, the (Cu+)/(Cu+ + Cu2+) ratio decreases.

The role of superoxide and hydroperoxide in the reductive activation of tryptophan-2,3-dioxygenase.

Radiocopper in L-tryptophan 2,3-dioxygenase isolated from Pseudomonas acidovorans grown in the presence of 64Cu (II).

  • F. O. Brady
  • Biology
    The Journal of biological chemistry
  • 1975

The nature and mechanism of the tryptophan pyrrolase (peroxidase-oxidase) reaction of Pseudomonas and of rat liver.

Spectral studies on the catalytic mechanism and activation of Pseudomonas tryptophan oxygenase (tryptophan pyrrolase).

Tryptophan oxygenase of Pseudomonas acidovorans. Purification, composition, and subunit structure.

Optical and electron paramagnetic resonance spectral data indicate that the single protoheme iron moiety of both the native (ferric) and the chemically reduced (ferrous) form of the holoenzyme exists predominantly in the high spin configuration.

Pyrrolooxygenase: its action on tryptophan-containing enzymes and peptides.