부산대학교 도서관

Thiamin pyrophosphate is an essential coenzyme in all organisms that depend on fermentation, respiration or photosynthesis to produce ATP, It is synthesized through two independent biosynthetic routes: one for the synthesis of 2-methyl-4-amino-5-hydroxymethylpyrimidine pyrophosphate (pyrimidine moiety) and another for the synthesis of 4-methyl-5-(β-hydroxy-ethyl) thiazole phosphate (thiazole moiety). Herein, we will describe the three-dimensional structure of TH11 protein from Arabidopsis thaliana determined by single wavelength anomalous diffraction to 1.6 Å resolution. The protein was produced using heterologous expression in bacteria, unexpectedly bound to 2-carboxyIate-4-methyl-5-β-(ethyl adenosine 5′-diphosphate) thiazole, a potential intermediate of the thiazole biosynthesis in Eukaryotes. TH11 has a topology similar to dinucleotide binding domains and although details concerning its function are unknown, this work provides new clues about the thiazole biosynthesis in Eukaryotes. [ABSTRACT FROM AUTHOR]