4.2 Review

A unique mechanism for thiolation of serum albumins by disulphide molecules

期刊

JOURNAL OF BIOCHEMISTRY
卷 167, 期 2, 页码 165-171

出版社

OXFORD UNIV PRESS
DOI: 10.1093/jb/mvz084

关键词

disulphide molecules; protein thiolation; serum albumin

资金

  1. Ministry of Education, Sciences, Sports, Technology (MEXT), Japan [26252018, 26111011]
  2. JST PRESTO program
  3. Japan Society for the Promotion of Science
  4. Program for Leading Graduate Schools Integrative Graduate Education and Research in Green Natural Sciences'', MEXT, Japan
  5. Grants-in-Aid for Scientific Research [26252018, 26111011] Funding Source: KAKEN

向作者/读者索取更多资源

Protein S-thiolation is a reversible oxidative modification that serves as an oxidative regulatory mechanism for certain enzymes and binding proteins with reactive cysteine residues. It is generally believed that the thiolation occurs at free sulphydryl group of cysteine residues. Meanwhile, despite the fact that disulphide linkages, serving structural and energetic roles in proteins, are stable and inert to oxidative modification, a recent study shows that the thiolation could also occur at protein disulphide linkages when human serum albumin (HSA) was treated with disulphide molecules, such as cystine and homocystine. A chain reaction mechanism has been proposed for the thiolation at disulphide linkages, in which free cysteine (Cys34) is involved in the reaction with disulphide molecules to form free thiols (cysteine or homocysteine) that further react with protein disulphide linkages to form the thiolated cysteine residues in the protein. This review focuses on the recent finding of this unique chain reaction mechanism of protein thiolation.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.2
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据