期刊
JOURNAL OF ANTIBIOTICS
卷 67, 期 1, 页码 65-70出版社
SPRINGERNATURE
DOI: 10.1038/ja.2013.88
关键词
Escherichia coli; glycosyltransferase; tetracycline
资金
- NSF CBET
- David and Lucile Packard Foundation Fellowship
- Div Of Chem, Bioeng, Env, & Transp Sys
- Directorate For Engineering [1159759] Funding Source: National Science Foundation
Glycosylation with deoxysugar is a common strategy used by nature to introduce structural diversity and biological activities among natural products. In this study, we biochemically confirmed the activities of SsfS6, a C-glycosyltransferase in the SF2575 biosynthetic pathway, as a regioselective D-olivose transferase that acts on the C-9 position of an anhydrotetracycline aglycon. To perform the glycosyl transfer reaction using Escherichia coli as a whole-cell biocatalyst, we reconstituted the biosynthesis of TDP-D-olivose using a heterologous pathway. Under in vivo conditions, SsfS6 transferred multiple endogenous sugar substrates, in addition to D-olivose, to the anhydrotetracycline substrate, demonstrating broad substrate tolerance and potential as a tetracycline-diversifying enzyme.
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