Cited by 367Metal-Catalyzed Oxygenation MechanismsAmino Acid Enzymes and MetabolismHemoglobin structure and function

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Indoleamine 2,3-dioxygenase. Purification and some properties

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Shimizu, T., Nomiyama, S., Hirata, F., Hayaishi, O.·1978·Journal of Biological Chemistry

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Abstract

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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Background
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Background
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Indoleamine dioxygenase and tryptophan dioxygenase activities are regulated through GAPDH- and Hsp90-dependent control of their heme levels
Biswas, P., Dai, Y., & Stuehr, D. J. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.01.008 · Cited by 31
Linking phencyclidine intoxication to the tryptophan‐kynurenine pathway: Therapeutic implications for schizophrenia
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Selective inhibition of IDO1, D-1-methyl-tryptophan (D-1MT), effectively increased EpCAM/CD3-bispecific BiTE antibody MT110 efficacy against IDO1hibreast cancer via enhancing immune cells activity
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Indoleamine dioxygenase and tryptophan dioxygenase activities are regulated through control of cell heme allocation by nitric oxide
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Apicomplexan Parasite, Eimeria falciformis, Co-opts Host Tryptophan Catabolism for Life Cycle Progression in Mouse
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[26] Indoleamine 2,3-dioxygenase
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Self-citation
Addition of an Indoleamine-2,3,-dioxygenase Inhibitor to B cell Depletion Therapy Blocks Autoreactive B Cell Activation and Recurrence of Arthritis
Pigott, E., & Mandik-Nayak, L. (2012) · Arthritis & Rheumatism · doi:10.1002/art.34406 · Cited by 27
“IDO is an IFN-γ inducible enzyme that catalyzes the initial and rate-limiting step in tryptophan degradation (11).”
Background
Metabolism and Biology of Tryptophan
Brown, R. R. (1996) · Advances in experimental medicine and biology · doi:10.1007/978-1-4613-0381-7_2 · Cited by 22
Structural Study of a Flexible Active Site Loop in Human Indoleamine 2,3-Dioxygenase and Its Functional Implications
Álvarez, L., Lewis-Ballester, A., Roitberg, A. E., Estrin, D. A., Yeh, S., Marti, M. A., & Capece, L. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00077 · Cited by 32
Inhibition of indoleamine 2,3-dioxygenase prevented cognitive impairment in adult Wistar rats subjected to pneumococcal meningitis
Barichello, T., Generoso, J. S., Simões, L. R., Galvão-Elias, S., Tashiro, M. H., Dominguini, D., Comim, C. M., Vilela, M. C., Teixeira, A. L., & Quevedo, J. (2013) · Translational research · doi:10.1016/j.trsl.2013.08.001 · Cited by 25
Beyond immunosuppression: reconsidering indoleamine 2,3-dioxygenase as a pathogenic element of chronic inflammation
Muller, A., Mandik-Nayak, L., & Prendergast, G. (2010) · Immunotherapy · doi:10.2217/imt.10.22 · Cited by 26
“IDO catalyzes the initial and rate-limiting step in the degradation of tryptophan along a pathway that can lead to the biosynthesis of NAD+ [4].”
BackgroundInfluential
Double Mechanism for Apical Tryptophan Depletion in Polarized Human Bronchial Epithelium
Zegarra‐Moran, O., Folli, C., Manzari, B., Ravazzolo, R., Varesio, L., & Galietta, L. J. V. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.1.542 · Cited by 23
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Elevated interleukin‐27 levels in human neonatal macrophages regulate indoleamine dioxygenase in a STAT ‐1 and STAT ‐3‐dependent manner
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“Indoleamine dioxygenase (IDO) catalyzes the oxidative cleavage of the 2,3 double bond in the indole ring of tryptophan.(1) Tryptophan catabolism via the IDO pathway has been shown to be necessary for immune tolerance of the semi-allogeneic but not syngeneic murine fetus.”
Background
Indoleamine 2,3-Dioxygenase (IDO) Activity: A Perspective Biomarker for Laboratory Determination in Tumor Immunotherapy
Yang, P., & Zhang, J. (2023) · Biomedicines · doi:10.3390/biomedicines11071988 · Cited by 28
A new regime of heme-dependent aromatic oxygenase superfamily
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Discovery of IACS-9779 and IACS-70465 as Potent Inhibitors Targeting Indoleamine 2,3-Dioxygenase 1 (IDO1) Apoenzyme
Hamilton, M. M., Mseeh, F., McAfoos, T. J., Leonard, P. G., Reyna, N. J., Harris, A. L., Xu, A., Han, M., Soth, M., Czakó, B., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00679 · Cited by 28
Specific induction of pulmonary indoleamine 2,3-dioxygenase by bacterial lipopolysaccharide.
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Self-citation
Human Primary CD4+ T Cells Activated in the Presence of IFN-α2b Express Functional Indoleamine 2,3-Dioxygenase
Curreli, S., Romerio, F., Mirandola, P., Barion, P., Bemis, K., & Zella, D. (2001) · Journal of Interferon and Cytokine Research · doi:10.1089/107999001750277916 · Cited by 24
Inhibition of Type I Collagen mRNA Expression Independent of Tryptophan Depletion in Interferon-γ-Treated Human Dermal Fibroblasts
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Transcriptomic analysis of interferon-γ-regulated genes in endometrial explants and their possible role in regulating maternal endometrial immunity during the implantation period in pigs, a true epitheliochorial placentation species
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Comparison of the sequences of Turbo and Sulculus indoleamine dioxygenase-like myoglobin genes.
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Spectroscopic and equilibrium properties of the indoleamine 2,3-dioxygenase-tryptophan-O2 ternary complex and of analogous enzyme derivatives. Tryptophan binding to ferrous enzyme adducts with dioxygen, nitric oxide, and carbon monoxide.
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Constructing manmade enzymes for oxygen activation
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How is the distal pocket of a heme protein optimized for binding of tryptophan?
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Decreased indoleamine 2,3-dioxygenase expression in dendritic cells and role of indoleamine 2,3-dioxygenase-expressing dendritic cells in immune thrombocytopenia
Xu, S.-Q., Wang, C.-Y., Zhu, X., Dong, X.-Y., Shi, Y., Peng, J., Qin, P., Sun, J.-Z., Guo, C., Ni, H., et al. (2012) · Annals of Hematology · doi:10.1007/s00277-012-1451-0 · Cited by 22
“Together, this leads to apoptosis and inhibition of Tcells proliferation [2, 3].”
Background
NADH Oxidase Activity of Indoleamine 2,3-Dioxygenase*
Rosell, F., Kuo, H. H., & Mauk, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.262139 · Cited by 22
Cooperative binding of L-trp to human tryptophan 2,3-dioxygenase: resonance Raman spectroscopic analysis.
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Shifting the balance of brain tryptophan metabolism elicited by isolation housing and systemic administration of lipopolysaccharide in mice
Miura, H., Shirokawa, T., Isobe, K., & Ozaki, N. (2008) · Stress · doi:10.1080/10253890802252442 · Cited by 25
“Because IDO can directly metabolize 5-HT (Shimizu et al. 1978), the activated IDO may decrease the 5-HT level (Muller and Schwarz 2007).”
Background
Mechanisms by which acyclovir reduces the oxidative neurotoxicity and biosynthesis of quinolinic acid.
Müller, A. C., Dairam, A., Limson, J., & Daya, S. (2007) · Life Science · doi:10.1016/j.lfs.2006.11.031 · Cited by 22
A myoglobin evolved from indoleamine 2,3-dioxygenase, a tryptophan-degrading enzyme.
Suzuki, T., Kawamichi, H., & Imai, K. (1998) · Comparative Biochemistry and Physiology Part B Comparative Biochemistry · doi:10.1016/s0305-0491(98)10086-x · Cited by 22
Managing epilepsy-associated depression: Serotonin enhancers or serotonin producers?
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Authors: Shimizu, T., Nomiyama, S., Hirata, F., & Hayaishi, O.
Affiliations: Kyoto University (JP)
ORCID: Shimizu, T.
Hirata, F.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1978-07
Volume: 253
Issue: 13
Pages: 4700-4706
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(17)30447-7
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 15461 d)
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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Indoleamine 2,3-dioxygenase. Purification and some properties

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