Title of article :
Thi20, a remarkable enzyme from Saccharomyces cerevisiae with dual thiamin biosynthetic and degradation activities
Author/Authors :
Haas، نويسنده , , Amy L. and Laun، نويسنده , , Nathan P. and Begley، نويسنده , , Tadhg P.، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2005
Abstract :
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 II 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.
Keywords :
4-Amino-2-methyl-5-hydroxymethylpyrimidine kinase , thiamin , Thiamin metabolism , thiamin biosynthesis , Thiamin degradation , Thiaminase II
Journal title :
Bioorganic Chemistry: an International Journal
Journal title :
Bioorganic Chemistry: an International Journal