2016 Fiscal Year Final Research Report
Biosynthetic enzymes for streptothricin group antibiotic
| Project/Area Number |
15K14724
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Bioorganic chemistry
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| Research Institution | Fukui Prefectural University |
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Principal Investigator |
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| Project Period (FY) |
2015-04-01 – 2017-03-31
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| Keywords | ペプチド結合 / tRNA |
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| Outline of Final Research Achievements |
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.
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| Free Research Field |
応用微生物学
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