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Unraveling the specificities of the different human methionine sulfoxide reductases

Elien Vandermarliere (UGent) , Bart Ghesquière (UGent) , Veronique Jonckheere (UGent) , Kris Gevaert (UGent) and Lennart Martens (UGent)
(2014) PROTEOMICS. 14(17-18). p.1990-1998
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Abstract
The oxidation of free and protein-bound methionine into methionine sulfoxide is a frequently occurring modification caused by ROS. Most organisms express methionine sulfoxide reductases (MSR enzymes) to repair this potentially damaging modification. Humans express three different MSRB enzymes which reside in different cellular compartments. In this study, we have explored the specificity of the human MSRB enzymes both by in silico modeling and by experiments on oxidized peptides. We found that MSRB1 is the least specific MSRB enzyme, which is in agreement with the observation that MSRB1 is the only MSRB enzyme found in the cytosol and the nucleus, and therefore requires a broad specificity to reduce all possible substrates. MSRB2 and MSRB3, which are both found in mitochondria, are more specific but because of their co-occurrence they can likely repair all possible substrates.
Keywords
MSRA, SYSTEM, PROTEIN, FORCE-FIELD, OXIDATIVE STRESS, ESCHERICHIA-COLI, REDUCTION, RESIDUES, Technology, CATALYTIC MECHANISM, Specificity, Oxidized methionine, Methionine sulfoxide reductase, In silico analysis, DAMAGE

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Chicago
Vandermarliere, Elien, Bart Ghesquière, Veronique Jonckheere, Kris Gevaert, and Lennart Martens. 2014. “Unraveling the Specificities of the Different Human Methionine Sulfoxide Reductases.” Proteomics 14 (17-18): 1990–1998.
APA
Vandermarliere, E., Ghesquière, B., Jonckheere, V., Gevaert, K., & Martens, L. (2014). Unraveling the specificities of the different human methionine sulfoxide reductases. PROTEOMICS, 14(17-18), 1990–1998.
Vancouver
1.
Vandermarliere E, Ghesquière B, Jonckheere V, Gevaert K, Martens L. Unraveling the specificities of the different human methionine sulfoxide reductases. PROTEOMICS. 2014;14(17-18):1990–8.
MLA
Vandermarliere, Elien, Bart Ghesquière, Veronique Jonckheere, et al. “Unraveling the Specificities of the Different Human Methionine Sulfoxide Reductases.” PROTEOMICS 14.17-18 (2014): 1990–1998. Print.
@article{5822277,
  abstract     = {The oxidation of free and protein-bound methionine into methionine sulfoxide is a frequently occurring modification caused by ROS. Most organisms express methionine sulfoxide reductases (MSR enzymes) to repair this potentially damaging modification. Humans express three different MSRB enzymes which reside in different cellular compartments. In this study, we have explored the specificity of the human MSRB enzymes both by in silico modeling and by experiments on oxidized peptides. We found that MSRB1 is the least specific MSRB enzyme, which is in agreement with the observation that MSRB1 is the only MSRB enzyme found in the cytosol and the nucleus, and therefore requires a broad specificity to reduce all possible substrates. MSRB2 and MSRB3, which are both found in mitochondria, are more specific but because of their co-occurrence they can likely repair all possible substrates.},
  author       = {Vandermarliere, Elien and Ghesqui{\`e}re, Bart and Jonckheere, Veronique and Gevaert, Kris and Martens, Lennart},
  issn         = {1615-9853},
  journal      = {PROTEOMICS},
  keyword      = {MSRA,SYSTEM,PROTEIN,FORCE-FIELD,OXIDATIVE STRESS,ESCHERICHIA-COLI,REDUCTION,RESIDUES,Technology,CATALYTIC MECHANISM,Specificity,Oxidized methionine,Methionine sulfoxide reductase,In silico analysis,DAMAGE},
  language     = {eng},
  number       = {17-18},
  pages        = {1990--1998},
  title        = {Unraveling the specificities of the different human methionine sulfoxide reductases},
  url          = {http://dx.doi.org/10.1002/pmic.201300357},
  volume       = {14},
  year         = {2014},
}

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