期刊
ACS SYNTHETIC BIOLOGY
卷 6, 期 3, 页码 421-427出版社
AMER CHEMICAL SOC
DOI: 10.1021/acssynbio.6b00341
关键词
antibiotic; kirromycin; polyketide synthase; trans-acyltransferase; engineering click chemistry
资金
- German Center for Infection Research (Deutsches Zentrum fur Infektionsforschung, DZIF) [TTU09.802, TTU09.704]
- Novo Nordisk Foundation [NNF15OC0016226]
- National Institute of Health [GM104258-01]
- NNF Center for Biosustainability [New Bioactive Compounds] Funding Source: researchfish
- Novo Nordisk Fonden [NNF15OC0016226, NNF10CC1016517] Funding Source: researchfish
During polyketide biosynthesis, acyltransferases (ATs) are the essential gatekeepers which provide the assembly lines with precursors and thus contribute greatly to structural diversity. Previously, we demonstrated that the discrete AT KirCII from the kirromycin antibiotic pathway accesses nonmalonate extender units. Here, we exploit the promiscuity of KirCII to generate new kirromycins with allyl- and propargyl-side chains in vivo, the latter were utilized as educts for further modification by click chemistry.
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