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

Molecules

Jason Ching-Yao Lin¹  Bing-Yu Chiang¹  Chi-Chi Chou¹  Tzu-Chieh Chen¹  Yi-Ju Chen³  Yu-Ju Chen³  Chun-Hung Lin¹  Noriyuki Nagahara² 

[1] Institute of Biological Chemistry, Academia Sinica, 128 Academia Road Section 2, Taipei 11529, Taiwan; E-Mails:Institute of Biological Chemistry, Academia Sinica, 128 Academia Road Section 2, Taipei 11529, Taiwan;;Institute of Chemistry, Academia Sinica, 128 Academia Road Section 2, Taipei 11529, Taiwan; E-Mails:

关键词: glutathione;    redox;    proteomics;    glutathionylation;    transglutaminase;   

DOI  :  10.3390/molecules20011452

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.