The DOI matches its Crossref record; 35 of the 38 references it cites were found in a registry or an index.
Indoleamine 2,3-dioxygenase. Purification and some properties
Open accessAbstract
Indoleamine 2,3-dioxygenase was purified from rabbit small intestine to apparent homogeneity as judged by polyacrylamide gel electrophoresis and analytical ultracentrifugation. The native enzyme was a monomeric protein of a molecular weight of 41,000 +/- 1,000 with an s020,w value of 3.45 S. It had a relative abundance of hydrophobic amino acids such as valine, leucine, and isoleucine, and contained approximately 5% carbohydrate by weight. The estimated content of sugar residues per mol of enzyme was: galactose, 1.2; mannose, 2.6; N-acetylglucosamine, 5.2; and sialic acid, 0.8. One mole of enzyme had 0.8 mol of protoheme IX as a prosthetic group. However, copper was not detected in a significant amount and the ratio of copper to heme was less than 0.03. EPR spectra of the nitric oxide complex of the ferrous enzyme indicated that a nitrogen atom, possibly in an imidazole group, might be coordinated as the fifth ligand of the heme coenzyme. The anisotropic g values were gx = 2.08, gy = 1.98, and gz = 2.01. A single enzyme protein catalyzed the oxygenative ring cleavage of D- and L-tryptophan, D- and L-5-hydroxytryptophan, tryptamine, and serotonin. In addition, the purified enzyme had a peroxidase activity with guaiacol and potassium iodide as hydrogen donors, but not a catalase activity.
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“Increased IDO expression is responsible for the catabolism of TRP in the KYN degradation pathway [36] and is canonically upregulated by inflammatory mechanisms [37,38].”
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Items 301–308 of 308
Immune Checkpoint Combinations with Inflammatory Pathway Modulators
DeVito, N. C., Morse, M. A., Hanks, B. A., & Clarke, J. M. (2017) · Current cancer research · doi:10.1007/978-3-319-63757-0_8
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Zhang, Y. (2014) · doi:10.14288/1.0165570
“However, Kyn as the metabolite of Trp has also been detected in many other tissues, such as intestine, suggesting that another enzyme responsible for catabolizing Trp can be expressed in the extrahepatic tissues [378,379].”
BackgroundReactivities of indoleamine 2,3-dioxygenases
Kuo, H. H. (2013) · doi:10.14288/1.0071925
“For example, using MCD spectroscopy to study the effects of L-Trp binding to rabbit IDOFe3+CN and IDOFe2+CO, Uchida and co-workers observed a decrease in the Soret band intensity, which they attribute to a shift from linear conformations of the FeCO or FeCN bonds to bent conformations due to steric constraints imposed…”
BackgroundInfluentialPschowski, R. (2012) · Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver · doi:10.17169/refubium-8403
Indoleamine 2,3-Dioxygenase in Immune Escape: Regulation and Therapeutic Inhibition
Muller, A. J., & Prendergast, G. C. (2007) · Elsevier eBooks · doi:10.1016/b978-012372551-6/50083-3
Indoleamine-pyrrole 2,3-dioxygenase
Schomburg, D., & Stephan, D. (1994) · doi:10.1007/978-3-642-57942-4_41
Metadata
- Authors
- Shimizu, T., Nomiyama, S., Hirata, F., & Hayaishi, O.
- Affiliations
- Kyoto University (JP)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1978-07
- Volume
- 253
- Issue
- 13
- Pages
- 4700-4706
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1607682771
- Cited by
- 367
- References
- 38
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 6 · 2023: 5 · 2022: 3 · 2021: 14 · 2020: 9 · 2019: 10 · 2018: 9 · 2017: 13 · 2016: 15 · 2015: 12 · 2014: 13 · 2013: 12 · 2012: 20
- FWCI
- 5.77
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Keywords
- indoleamine 2,3-dioxygenase, enzyme purification, rabbit small intestine, protoheme, sialic acid, carbohydrate content, protein secondary structure, electron spin resonance, tryptophan oxidation, serotonin oxidation, peroxidase activity, guaiacol
- MeSH terms
- Amino Acids, Animals, Electrophoresis, Disc, Hexoses, Hydrogen-Ion Concentration, Indoles, Intestine, Small, Molecular Weight, Oxygenases, Rabbits, Seasons, Substrate Specificity
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