Research Project
Grant-in-Aid for Challenging Exploratory Research
The antibiotic streptothricin (ST) possesses an amino sugar bound to an L-β-lysine (β-Lys) residue via a peptide bond. The peptide-bond formation has been shown to be catalyzed by a nonribosomal peptide synthetase (NRPS) during ST biosynthesis. The focus of this study is the closely related ST analogue BD-12, which carries a glycine-derived side chain rather than a β-Lys residue. In the biosynthetic studies of BD-12, we revealed that the peptide bond between the amino sugar and the glycine residue is catalyzed by a Fem-like enzyme (Orf 11) in a tRNA-dependent manner rather than by an NRPS; Orf 11 utilizes Gly-tRNA as a substrate.From a genome database, we further identified the enzyme (Sba18) homologous to Orf11 and investigated the substrate specificity. Interestingly, Sba18 was found to accept Ala-tRNA and Ser-tRNA as well as Gly-tRNA, producing new ST-related compounds which carry alanine and serine side chains.
All 2016 2015
All Journal Article (1 results) (of which Peer Reviewed: 1 results, Open Access: 1 results, Acknowledgement Compliant: 1 results) Presentation (7 results)
Appl. Environ. Microbiol.
Volume: 82 Issue: 12 Pages: 3640-3648
10.1128/aem.00725-16
