期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 136, 期 2, 页码 566-569出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja409409h
关键词
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资金
- BBSRC
- Glycovaxyn
- Royal Society-Wolfson Merit Research Award
- Biotechnology and Biological Sciences Research Council [BB/E004350/1, BB/D005949/1, BB/C510824/1, BB/J009725/1, EGA17763] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/D023343/1, EP/E000614/1, EP/D023335/1, GR/T26542/01, EP/G026688/1, EP/I500200/1] Funding Source: researchfish
- BBSRC [BB/J009725/1, BB/E004350/1, BB/D005949/1] Funding Source: UKRI
- EPSRC [EP/E000614/1, EP/I500200/1, EP/G026688/1] Funding Source: UKRI
The lipid carrier specificity of the protein N-glycosylation enzyme. C. jejuni PglB was tested using a logical, synthetic array of natural and unnatural C10, C20, C30, and C40 polyisoprenol sugar pyrophosphates, including those bearing repeating cis-prenyl units. Unusual, short, synthetically accessible C20 prenols (nerylnerol 1d and geranylnerol 1e) were shown to be effective lipid carriers for PglB sugar substrates. Kinetic analyses for PglB revealed clear K-M-only modulation with lipid chain length, thereby implicating successful in vitro application at appropriate concentrations. This was confirmed by optimized, efficient in vitro synthesis allowing >90% of Asn-linked beta-N-GlcNAc-ylated peptide and proteins. This reveals a simple, flexible biocatalytic method for glycoconjugate synthesis using PglB N-glycosylation machinery and varied chemically synthesized glycosylation donor precursors.
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