No abstract

Rise and shine: Using a gene‐targeting approach aimed at identifying potential L‐threonine:uridine‐5′‐transaldolases that catalyze the formation of (5′S,6′S)‐C‐glycyluridine, a new bacterial translocase I inhibitor was discovered from an actinomycete following fermentation optimization.

No abstract

During the course of screening for translocase I inhibitors, the new liposidomycin-related compounds, A-90289 A and B, were isolated from a culture broth of Streptomyces sp. SANK 60405. The structural elucidations were carried out by NMR and high-resolution mass spectral analyses, and they were classified as members of the liponucleoside antibiotics group with a sulfate group at the C-2¢ position. A-90289 A and B inhibited bacterial translocase I with IC 50 values of 36.5 ng ml À1 and 33.8 ng ml À1 , respectively.

Bacterial phospho-N-acetylmuramyl-pentapeptide translocase (translocase I: EC 2.7.8.13) is a key enzyme in peptidoglycan biosynthesis, and a known target of antibiotics. Here we report a new nucleoside inhibitor for translocase I, A-102395, isolated from the culture broth of the strain Amycolatopsis sp. SANK 60206. A-102395 is a new derivative of capuramycin that has the benzene with a uniquely substituted chain instead of an aminocaprolactam. A-102395 is a potent inhibitor of bacterial translocase I with IC 50 value of 11 nM, but possesses no antimicrobial activity against various strains tested.