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Glutathionylspermidine in the Modification of Protein SH Groups: The Enzymology and Its Application to Study Protein Glutathionylation

1
Institute of Biological Chemistry, Academia Sinica, 128 Academia Road Section 2, Taipei 11529, Taiwan
2
The Core Facilities for Protein Structural Analysis, Academia Sinica, 128 Academia Road Section 2, Taipei 11529, Taiwan
3
Institute of Chemistry, Academia Sinica, 128 Academia Road Section 2, Taipei 11529, Taiwan
4
Department of Chemistry and Institute of Biochemical Sciences, National Taiwan University, Taipei 10617, Taiwan
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Academic Editors: Noriyuki Nagahara and Maria Wrobel
Molecules 2015, 20(1), 1452-1474; https://doi.org/10.3390/molecules20011452
Received: 30 September 2014 / Accepted: 15 December 2014 / Published: 15 January 2015
(This article belongs to the Special Issue Sulfur Atom: Element for Adaptation to an Oxidative Environment)
Cysteine is very susceptible to reactive oxygen species. In response; posttranslational thiol modifications such as reversible disulfide bond formation have arisen as protective mechanisms against undesired in vivo cysteine oxidation. In Gram-negative bacteria a major defense mechanism against cysteine overoxidation is the formation of mixed protein disulfides with low molecular weight thiols such as glutathione and glutathionylspermidine. In this review we discuss some of the mechanistic aspects of glutathionylspermidine in prokaryotes and extend its potential use to eukaryotes in proteomics and biochemical applications through an example with tissue transglutaminase and its S-glutathionylation. View Full-Text
Keywords: glutathione; redox; proteomics; glutathionylation; transglutaminase glutathione; redox; proteomics; glutathionylation; transglutaminase
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Lin, J.C.-Y.; Chiang, B.-Y.; Chou, C.-C.; Chen, T.-C.; Chen, Y.-J.; Chen, Y.-J.; Lin, C.-H. Glutathionylspermidine in the Modification of Protein SH Groups: The Enzymology and Its Application to Study Protein Glutathionylation. Molecules 2015, 20, 1452-1474.

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