Sensitive genome-wide screen for low secondary enzymatic activities: The YjbQ family shows thiamin phosphate synthase activity
Por:
Morett, E, Saab-Rincon, G, Olvera, L, Olvera, M, Flores, H, Grande, R
Publicada:
22 feb 2008
Categoría:
Molecular Biology
Resumen:
Contemporary enzymes are highly efficient and selective catalysts. However, due to the intrinsically very reactive nature of active sites, gratuitous secondary reactions are practically unavoidable. Consequently, even the smallest cell, with its limited enzymatic repertoire, has the potential to carry out numerous additional, very likely inefficient, secondary reactions. If selectively advantageous, secondary reactions could be the basis for the evolution of new fully functional enzymes. Here, we investigated if Escherichia coli has cryptic enzymatic activities related to thiamin biosynthesis. We selected this pathway because this vitamin is essential, but the cell's requirements are very small. Therefore, enzymes with very low activity could complement the auxotrophy of strains deleted of some bona fide thiamin biosynthetic genes. By overexpressing the E. coli's protein repertoire, we selected yjbQ, a gene that complemented a strain deleted of the thiamin phosphate synthase (TPS)-codi
Filiaciones:
Morett, E:
Univ Nacl Autonoma Mexico, Inst Biotechnol, Dept Ingn Celular & Biocatalists, Cuernavaca 62191, Morelos, Mexico
Saab-Rincon, G:
Univ Nacl Autonoma Mexico, Inst Biotechnol, Dept Ingn Celular & Biocatalists, Cuernavaca 62191, Morelos, Mexico
Olvera, L:
Univ Nacl Autonoma Mexico, Inst Biotechnol, Dept Ingn Celular & Biocatalists, Cuernavaca 62191, Morelos, Mexico
Olvera, M:
Univ Nacl Autonoma Mexico, Inst Biotechnol, Dept Ingn Celular & Biocatalists, Cuernavaca 62191, Morelos, Mexico
Flores, H:
Univ Nacl Autonoma Mexico, Inst Biotechnol, Dept Ingn Celular & Biocatalists, Cuernavaca 62191, Morelos, Mexico
Grande, R:
Univ Nacl Autonoma Mexico, Inst Biotechnol, Dept Ingn Celular & Biocatalists, Cuernavaca 62191, Morelos, Mexico
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