Thi20, a remarkable enzyme from Saccharomyces cerevisiae with dual thiamin biosynthetic and degradation activities.

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.

authors

• Begley, Tadhg

published proceedings

• Bioorg Chem

author list (cited authors)

• Haas, A. L., Laun, N. P., & Begley, T. P.

citation count

• 23

complete list of authors

• Haas, Amy L||Laun, Nathan P||Begley, Tadhg P

publication date

• January 2005

publisher

• Elsevier  Publisher

published in

• Bioorganic Chemistry  Journal

keywords

• Amino Acid Sequence
• Catalysis
• Chromatography, High Pressure Liquid
• Hydrolases
• Molecular Sequence Data
• Phosphotransferases
• Pyrimidines
• Saccharomyces Cerevisiae
• Sequence Alignment
• Thiamine

Digital Object Identifier (DOI)

• 10.1016/j.bioorg.2005.04.001

start page

• 338

end page

• 344

volume

• 33

issue

• 4

URL

• http%3A%2F%2Fdx.doi.org%2F10.1016%2Fj.bioorg.2005.04.001