User:Emma Ste.Marie/Sandbox 1
From Proteopedia
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| + | == Introduction == | ||
| + | Mammalian Thioredoxin reductases (mTRs) are a family of selenium-containing pyridine nucleotide-disulphide oxidoreductases with mechanistic similarities to glutathione reductases [1]. mTRs catalyse the NADPH-dependent reduction of the redox protein thioredoxin (Trx), as well as of other endogenous and exogenous compounds [1]. Unlike glutathione reductase or Escherichia coli (E. coli) thioredoxin reductase, mTRs contain a second redox-active site: A C-terminal Gly-Cys-Sec-Gly motif in which the penultimate Sec residue and the neighboring Cys residue exist in an 8-membered ring containing a selenosulfide bond in its reduced state [2,3]. | ||
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== References == | == References == | ||
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| + | 1.Mustacich, D.; Powis, G., Thioredoxin reductase. Biochemical Journal 2000, 346 (1), 1-8. | ||
| + | 2. Lothrop, A. P.; Snider, G. W.; Flemer Jr, S.; Ruggles, E. L.; Davidson, R. S.; Lamb, A. L.; Hondal, R. J., Compensating for the absence of selenocysteine in high-molecular weight thioredoxin reductases: the electrophilic activation hypothesis. Biochemistry 2014, 53 (4), 664-674. | ||
| + | 3. Ruggles, E. L.; Deker, P. B.; Hondal, R. J., Conformational analysis of oxidized peptide fragments of the C‐terminal redox center in thioredoxin reductases by NMR spectroscopy. Journal of Peptide Science 2014, 20 (5), 349-360. | ||
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Revision as of 21:42, 11 April 2018
Introduction
Mammalian Thioredoxin reductases (mTRs) are a family of selenium-containing pyridine nucleotide-disulphide oxidoreductases with mechanistic similarities to glutathione reductases [1]. mTRs catalyse the NADPH-dependent reduction of the redox protein thioredoxin (Trx), as well as of other endogenous and exogenous compounds [1]. Unlike glutathione reductase or Escherichia coli (E. coli) thioredoxin reductase, mTRs contain a second redox-active site: A C-terminal Gly-Cys-Sec-Gly motif in which the penultimate Sec residue and the neighboring Cys residue exist in an 8-membered ring containing a selenosulfide bond in its reduced state [2,3].
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References
1.Mustacich, D.; Powis, G., Thioredoxin reductase. Biochemical Journal 2000, 346 (1), 1-8. 2. Lothrop, A. P.; Snider, G. W.; Flemer Jr, S.; Ruggles, E. L.; Davidson, R. S.; Lamb, A. L.; Hondal, R. J., Compensating for the absence of selenocysteine in high-molecular weight thioredoxin reductases: the electrophilic activation hypothesis. Biochemistry 2014, 53 (4), 664-674. 3. Ruggles, E. L.; Deker, P. B.; Hondal, R. J., Conformational analysis of oxidized peptide fragments of the C‐terminal redox center in thioredoxin reductases by NMR spectroscopy. Journal of Peptide Science 2014, 20 (5), 349-360.
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
