A potent inhibitor of seryl tRNAsynthetase, designated SB-217452 has been isolated from Streptomyces sp. ATCC 700974. The fermentation, isolation, structure elucidation and some properties are described. SB-217452 showed inhibitory activity against both Staphylococcus aureus and rat seryl tRNA synthetases, with similar IC50 values of approximately 8 nM. The inhibitor is the serine linked nucleoside moiety of the antibiotic albomycin 82. In contrast to albomycin 52, SB-217452 showed only very weak antibacterial activity against a limited range of microorganisms. The compoundhas not been previously reported as a naturally occurring metabolite. In addition to SB-217452, albomycin S2 Fe3+ complex and the novel Al3+ complex were isolated from the fermentation. These complexes had no seryl tRNAsynthetase inhibitory activity. Aminoacyl-tRNA synthetases catalyze one of the most critical steps in protein biosynthesis. They attach one of twenty amino acids to one of about sixty tRNAs. Their specificities with regard to amino acids and tRNAs are responsible for the accurate primary structures of proteins. The enzymes are essential for cell viability, and are

Two novel inhibitors of isoleucyl tRNA synthetase designated SB-203207 and SB-203208 have been detected in the culture of a new Streptomyces species. The fermentation, isolation and someproperties of the inhibitors are described.

No abstract

ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.

A Potent Seryl tRNA Synthetase Inhibitor SB-217452 Isolated from a Streptomyces Species.-The production, isolation, identification, structure elucidation, and biological properties of the novel metabolite of the title inhibitor are described. -(STEFANSKA, ANNA L.; FULSTON, MARK; HOUGE-FRYDRYCH, CATHERINE S.V.; JONES, JO J.; WARR, STEPHEN R.; J.