Human Placenta Thioredoxin Reductase
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 273, Issue: 32, Page: 20096-20101
1998
- 474Citations
- 142Captures
- 1Mentions
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations474
- Citation Indexes474
- 474
- CrossRef411
- Captures142
- Readers142
- 83
- 59
- Mentions1
- References1
- Wikipedia1
Article Description
Human thioredoxin reductase is a pyridine nucleotide-disulfide oxidoreductase closely related to glutathione reductase but differing from the latter in having a Cys-SeCys (selenocysteine) sequence as an additional redox center. Because selenoproteins cannot be expressed yet in heterologous systems, we optimized the purification of the protein from placenta with respect to final yield (1–2 mg from one placenta), specific activity (42 units/mg), and selenium content (0.94 ± 0.03 mol/mol subunit). The steady state kinetics showed that the enzyme operates by a ping-pong mechanism; the value of k cat was 3330 ± 882 min −1, and the K m values were 18 μ m for NADPH and 25 μ m for Escherichia coli thioredoxin. The activation energy of the reaction was found to be 53.2 kJ/mol, which allows comparisons of the steady state data with previous pre-steady state measurements. In its physiological, NADPH-reduced form, the enzyme is strongly inhibited by organic gold compounds that are widely used in the treatment of rheumatoid arthritis; for auranofin, the K i was 4 n m when measured in the presence of 50 μ m thioredoxin. At 1000-fold higher concentrations, that is at micromolar levels, the drugs also inhibited human glutathione reductase and the selenoenzyme glutathione peroxidase.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925818490308; http://dx.doi.org/10.1074/jbc.273.32.20096; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0032493647&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/9685351; https://linkinghub.elsevier.com/retrieve/pii/S0021925818490308; https://dx.doi.org/10.1074/jbc.273.32.20096
Elsevier BV
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