Thi20, a remarkable enzyme from Saccharomyces cerevisiae with dual thiamin biosynthetic and degradation activities
Thi20, a remarkable enzyme from Saccharomyces cerevisiae with dual thiamin biosynthetic and degradation activities
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DOI：
10.1016/j.bioorg.2005.04.001
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发表时间：
2005-08-01
影响因子：
5.1
通讯作者：
Begley, TP
中科院分区：
文献类型：
--
作者：
Haas, AL;Laun, NP;Begley, TP
酿酒酵母（Saccharomyces cerevisiae） Thi20是一种与枯草芽孢杆菌ThiD和TenA同源的融合蛋白。Thi20的n端与枯草芽孢杆菌ThiD序列具有显著的同源性，c端与枯草芽孢杆菌TenA序列具有显著的同源性。Thi20与硫胺素孵育后发现其具有硫胺酶11活性，与HMP（4-氨基-2-甲基-5-羟甲基嘧啶）和ATP孵育后发现其具有HMP激酶和HMP- p（4-氨基-2-甲基-5-羟甲基嘧啶磷酸）激酶活性。这表明Thi20是一种具有硫胺素生物合成和降解活性的三功能蛋白。(c) 2005爱思唯尔公司版权所有。
Saccharomyces cerevisiae Thi20 is a fusion protein with homology to Bacillus subtilis ThiD and TenA. The N-terminus of Thi20 has significant sequence homology to B. subtilis ThiD, while the C-terminus has homology to B. subtilis TenA. Incubation of Thi20 with thiamin reveals that it has thiaminase 11 activity, in addition, incubation of Thi20 with HMP (4-amino-2-methyl-5-hydroxymethylpyrimidine) and ATP reveals that it has HMP kinase and HMP-P (4-amino-2-methyl-5-hydroxymethylpyrimidine phosphate) kinase activity. This demonstrates that Thi20 is a trifunctional protein with thiamin biosynthetic and degradative activity. (c) 2005 Elsevier Inc. All rights reserved.