Biotechnology Bulletin ›› 2022, Vol. 38 ›› Issue (2): 237-244.doi: 10.13560/j.cnki.biotech.bull.1985.2021-0611

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Research Progress in the Post-translational Modification of Superoxide Dismutase

JIA Hai-hong(), LI Bing-qing()   

  1. Department of Microbiology,Institute of Basic Medicine,Shandong First Medical University & Shandong Academy of Medical Sciences,Jinan 250062
  • Received:2021-05-11 Online:2022-02-26 Published:2022-03-09
  • Contact: LI Bing-qing E-mail:jia11112222@126.com;bingqingsdu@163.com

Abstract:

Superoxide dismutase(SOD)is a kind of antioxidant metal enzyme in living organisms,which can catalyze the disproportionation of superoxide anion radicals to produce oxygen(O2)and hydrogen peroxide(H2O2),and plays an important role in the balance of oxidation and antioxidant in the body as well as is closely related to the occurrence and development of many diseases. The regulation of SOD enzyme activity has always been the focus of research,most of which focus on two aspects:transcription level(gene expression)and translation level(enzyme protein synthesis).With the development of research,it is found that post-translational modification of protein(PTM)has an important effect on the enzyme activity of SOD. In recent years,more and more attentions have been paid to the influence of protein post-translational modification on SOD enzyme activity. In this review,we summarized several ways of SOD post-translation modification,such as nitration,phosphorylation,S-glutathione,glycosylation,acetylation,sulfonic acid modification,sulfonic acid modification,SUMO modification,etc.,and discussed the effect of modification on SOD enzyme activity and its physiological significance. Also we prospected the development and challenges of SOD post-translational modification. It provides a theoretical basis for the research,treatment and development of targeted drugs of related diseases.

Key words: superoxide dismutase, post-translational modification of proteins, enzyme activity, new ways of post-translation modification