Occurrence of a putative ancient-like isomerase involved in histidine and tryptophan biosynthesis
UNSPECIFIED. (2003) Occurrence of a putative ancient-like isomerase involved in histidine and tryptophan biosynthesis. EMBO REPORTS, 4 (3). pp. 296-300. ISSN 1469-221XFull text not available from this repository.
Official URL: http://dx.doi.org/10.1038/sj.embor.embor771
We report the occurrence of an isomerase with a putative (betaalpha)(8)- barrel structure involved in both histidine and tryptophan biosynthesis in Streptomyces coelicolor A3(2) and Mycobacterium tuberculosis HR37Rv. Deletion of a hisA homologue (SCO2050) putatively encoding N'-[(5'-phosphoribosyl)formimino]-5 amino-imidazole-4-carboxamide ribonucleotide isomerase from the chromosome of S. coelicolor A3(2) generated a double auxotrophic mutant for histidine and tryptophan. The bifunctional gene SCO2050 and its orthologue Rv1603 from M. tuberculosis complemented both hisA and trpF mutants of Escherichia coli. Expression of the E. coli trpF gene in the S. coelicolor mutant only complemented the tryptophan auxotrophy, and the hisA gene only complemented the histidine auxotrophy. The discovery of this enzyme, which has a broad-substrate specificity, has implications for the evolution of metabolic pathways and may prove to be important for understanding the evolution of the (betaalpha)(8) -barrels.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
|Journal or Publication Title:||EMBO REPORTS|
|Publisher:||NATURE PUBLISHING GROUP|
|Number of Pages:||5|
|Page Range:||pp. 296-300|
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