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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Structure of the thiazole biosynthetic enzyme THI1 from Arabidopsis thaliana

Autor(es):
Godoi, Paulo H. C. ; Galhardo, Rodrigo S. ; Luche, Douglas D. ; Van Sluys, Marie-Anne ; Menck, Carlos F. M. [5] ; Oliva, Glaucius
Número total de Autores: 6
Tipo de documento: Artigo Científico
Fonte: Journal of Biological Chemistry; v. 281, n. 41, p. 30957-30966, Oct. 2006.
Área do conhecimento: Ciências Biológicas - Bioquímica
Assunto(s):Coenzimas   Tiamina pirofosfato   Plantas   Arabidopsis
Resumo

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-(BETA-hydroxyethyl) thiazole phosphate (thiazole moiety). Herein, we will describe the three-dimensional structure of THI1 protein from Arabidopsis thaliana determined by single wavelength anomalous diffraction to 1.6A resolution. The protein was produced using heterologous expression in bacteria, unexpectedly bound to 2-carboxylate-4-methyl-5-BETA-(ethyl adenosine 5-diphosphate) thiazole, a potential intermediate of the thiazole biosynthesis in Eukaryotes. THI1 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. (AU)

Processo FAPESP: 03/13255-5 - Genes de reparo de DNA: análise funcional e evolução
Beneficiário:Carlos Frederico Martins Menck
Linha de fomento: Auxílio à Pesquisa - Temático