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Lee, S.-R., Bar-Noy, S., Kwon, J., Levine, R. L., Stadtman, T. C., Rhee, S. G. (2000) 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. Proceedings of the National Academy of Sciences, 97 (6) 2521-2526 doi:10.1073/pnas.050579797

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Reference TypeJournal (article/letter/editorial)
TitleMammalian thioredoxin reductase: Oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity
JournalProceedings of the National Academy of Sciences
AuthorsLee, S.-R.Author
Bar-Noy, S.Author
Kwon, J.Author
Levine, R. L.Author
Stadtman, T. C.Author
Rhee, S. G.Author
Year2000 (March 14)Volume97
Issue6
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.050579797Search in ResearchGate
Generate Citation Formats
Mindat Ref. ID1652743Long-form Identifiermindat:1:5:1652743:2
GUID0
Full ReferenceLee, S.-R., Bar-Noy, S., Kwon, J., Levine, R. L., Stadtman, T. C., Rhee, S. G. (2000) 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. Proceedings of the National Academy of Sciences, 97 (6) 2521-2526 doi:10.1073/pnas.050579797
Plain TextLee, S.-R., Bar-Noy, S., Kwon, J., Levine, R. L., Stadtman, T. C., Rhee, S. G. (2000) 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. Proceedings of the National Academy of Sciences, 97 (6) 2521-2526 doi:10.1073/pnas.050579797
In(2000, March) Proceedings of the National Academy of Sciences Vol. 97 (6) Proceedings of the National Academy of Sciences

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Zhong, L., Arner, E. S. J., Holmgren, A. (2000) Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence. Proceedings of the National Academy of Sciences, 97 (11) 5854-5859 doi:10.1073/pnas.100114897
Gorlatov, S. N., Stadtman, T. C. (1998) Human thioredoxin reductase from HeLa cells: Selective alkylation of selenocysteine in the protein inhibits enzyme activity and reduction with NADPH influences affinity to heparin. Proceedings of the National Academy of Sciences, 95 (15) 8520-8525 doi:10.1073/pnas.95.15.8520
Gladyshev, V. N., Jeang, K. T., Stadtman, T. C. (1996) Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene. Proceedings of the National Academy of Sciences, 93 (12) 6146-6151 doi:10.1073/pnas.93.12.6146
Kwon, J., Lee, S.-R., Yang, K.-S., Ahn, Y., Kim, Y. J., Stadtman, E. R., Rhee, S. G. (2004) Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors. Proceedings of the National Academy of Sciences, 101 (47) 16419-16424 doi:10.1073/pnas.0407396101
Liu, S.-Y., Stadtman, T. C. (1997) Heparin-binding properties of selenium-containing thioredoxin reductase from HeLa cells and human lung adenocarcinoma cells. Proceedings of the National Academy of Sciences, 94 (12) 6138-6141 doi:10.1073/pnas.94.12.6138
Moskovitz, J., Bar-Noy, S., Williams, W. M., Requena, J., Berlett, B. S., Stadtman, E. R. (2001) Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals. Proceedings of the National Academy of Sciences, 98 (23) 12920-12925 doi:10.1073/pnas.231472998
Tamura, T., Stadtman, T. C. (1996) A new selenoprotein from human lung adenocarcinoma cells: purification, properties, and thioredoxin reductase activity. Proceedings of the National Academy of Sciences, 93 (3) 1006-1011 doi:10.1073/pnas.93.3.1006
Barglow, K. T., Knutson, C. G., Wishnok, J. S., Tannenbaum, S. R., Marletta, M. A. (2011) Site-specific and redox-controlled S-nitrosation of thioredoxin. Proceedings of the National Academy of Sciences, 108 (35) doi:10.1073/pnas.1110736108
Lacourciere, G. M., Stadtman, T. C. (1999) Catalytic properties of selenophosphate synthetases: Comparison of the selenocysteine-containing enzyme from Haemophilus influenzae with the corresponding cysteine-containing enzyme from Escherichia coli. Proceedings of the National Academy of Sciences, 96 (1) 44-48 doi:10.1073/pnas.96.1.44
Requena, J. R., Groth, D., Legname, G., Stadtman, E. R., Prusiner, S. B., Levine, R. L. (2001) Copper-catalyzed oxidation of the recombinant SHa(29-231) prion protein. Proceedings of the National Academy of Sciences, 98 (13) 7170-7175 doi:10.1073/pnas.121190898
Sandalova, T., Zhong, L., Lindqvist, Y., Holmgren, A., Schneider, G. (2001) Three-dimensional structure of a mammalian thioredoxin reductase: Implications for mechanism and evolution of a selenocysteine-dependent enzyme. Proceedings of the National Academy of Sciences, 98 (17) 9533-9538 doi:10.1073/pnas.171178698
 
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