作者
Tomasz Frączyk, Konrad Kubiński, Maciej Masłyk, Joanna Cieśla, Ulf Hellman, David Shugar, Wojciech Rode
发表日期
2010/6/1
期刊
Bioorganic chemistry
卷号
38
期号
3
页码范围
124-131
出版商
Academic Press
简介
Thymidylate synthase (TS) was found to be a substrate for both catalytic subunits of human CK2, with phosphorylation by CK2α and CK2α′ characterized by similar Km values, 4.6μM and 4.2μM, respectively, but different efficiencies, the apparent turnover number with CK2α being 10-fold higher. With both catalytic subunits, phosphorylation of human TS, like calmodulin and BID, was strongly inhibited in the presence of the regulatory subunit CK2β, the holoenzyme being activated by polylysine. Phosphorylation of recombinant human, rat, mouse and Trichinella spiralis TSs proteins was compared, with the human enzyme being apparently a much better substrate than the others. Following hydrolysis and TLC, phosphoserine was detected in human and rat, and phosphotyrosine in T. spiralis, TS, used as substrates for CK2α. MALDI-TOF MS analysis led to identification of phosphorylated Ser124 in human TS, within …
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