Glutathionylspermidine in the modification of protein SH groups: the enzymology and its application to study protein glutathionylation

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 cyste...

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Bibliographic Details
Published in:Molecules (Basel, Switzerland) Switzerland), 2015-01, Vol.20 (1), p.1452-1474
Main Authors: Lin, Jason Ching-Yao, Chiang, Bing-Yu, Chou, Chi-Chi, Chen, Tzu-Chieh, Chen, Yi-Ju, Chen, Yu-Ju, Lin, Chun-Hung
Format: Article
Language:English
Subjects:
glutathione
Glutathione - analogs & derivatives
Glutathione - metabolism
glutathionylation
Prokaryotic Cells - metabolism
Protein Processing, Post-Translational
Proteins - metabolism
proteomics
redox
Review
Spermidine - analogs & derivatives
Spermidine - metabolism
Sulfhydryl Compounds - metabolism
transglutaminase
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Summary: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.
ISSN:1420-3049
1420-3049
DOI:10.3390/molecules20011452