Mammalian thioredoxin reductase: Oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity-Reference-Cited by-同舟云学术

Mammalian thioredoxin reductase: Oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity

Published:2000-02-25 Issue:6 Volume:97 Page:2521-2526
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Lee S.-R.,Bar-Noy S.,Kwon J.,Levine R. L.,Stadtman T. C.,Rhee S. G.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference20 articles.

1. Sequence of thioredoxin reductase from Escherichia coli. Relationship to other flavoprotein disulfide oxidoreductases.

2. Thioredoxin-dependent peroxide reductase from yeast.

3. Rat liver thioredoxin and thioredoxin reductase: purification and characterization

4. A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity.

5. Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene.

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