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

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

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Shimizu, T., Nomiyama, S., Hirata, F., Hayaishi, O.·1978·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(17)30447-7
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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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Crossref · 10.1016/s0021-9258(17)30447-7

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35 of 35 references verified0 citation errors · 0 not checkable

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Citations

Cites

Research works printed but not linked: 12

  1. Yamamoto, 1967, J. Biol. Chem., 242, 5260, 10.1016/S0021-9258(18)99420-2 · DOI
  2. Hayaishi, 1975, FEBS Proc. Meet., 40, 131
  3. Knox, 1955, Methods Enzymol., 2, 246
  4. Gerlach, 1974, 2, 569
  5. Putter, 1974, 2, 685
  6. Chance, 1955, Methods Enzymol., 2, 764, 10.1016/S0076-6879(55)02300-8 · DOI
  7. Siegel, 1966, Biochem. Biophys. Acta, 112, 346
  8. Moore, 1963, J. Biol. Chem., 238, 235, 10.1016/S0021-9258(19)83985-6 · DOI
  9. Warren, 1959, J. Biol. Chem., 234, 1971, 10.1016/S0021-9258(18)69851-5 · DOI
  10. Yonetani, 1972, J. Biol. Chem., 247, 2447, 10.1016/S0021-9258(19)45449-5 · DOI
  11. Brady, 1976, 74, 343
  12. Hirata, 1976, 74, 354

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Metadata

Authors
Shimizu, T., Nomiyama, S., Hirata, F., & Hayaishi, O.
Affiliations
Kyoto University (JP)
ORCID
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
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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