68982-81-0

Usage

InChI:InChI=1/C20H35O4P/c1-17(2)9-6-10-18(3)11-7-12-19(4)13-8-14-20(5)15-16-24-25(21,22)23/h9,11,13,15H,6-8,10,12,14,16H2,1-5H3,(H2,21,22,23)/b18-11+,19-13+,20-15+

Upstream product

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• 25996-10-5 (Z)-neryl bromide 
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• 1528749-25-8 (2Z,6Z)-1-(tert-butyldiphenylsilyloxy)-3,7-dimethyl-8-(2-tetrahydropyranyloxy)octa-2,6-diene 
• 1528749-23-6 (Z)-1-O-tert-butyldiphenylsilyl-3-methyl-6-O-(4-toluenesulfonyl)hexa-2-en-1,6-diol 
• 1528749-22-5 (Z)-1-O-tert-butyldiphenylsilyl-3-methyl-6-O-(4-toluenesulfonyl)hexa-2-en-1,6-diol 
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• 139109-04-9 (Z)-1-[(tert-butyldiphenylsilyl)oxy]-3-methyl-2-hexen-6-al 
• 201670-51-1 (Z)-1-(tert-butyldiphenylsilyloxy)-6,7-epoxy-3,7-dimethylocta-2-ene 

Relevant academic research and scientific papers

N-GLYCOSYLATION OF PEPTIDES AND PROTEINS

A process for the production of a glycoconjugate by N-glycosylation of a protein or peptide comprising the sequence D/E-X-N-X-S/T, wherein each X is the same or different and is any natural amino acid other than proline, wherein the process comprises reacting the protein or peptide with a polyisoprenyl pyrophosphate of formula (I), or a salt thereof, in the presence of PglB: (I) to produce the glycoconjugate comprising the protein or peptide having a saccharide [SI] linked to the asparagine in the sequence D/E-X-N-X-S/T. Polyisoprenylpyrophosphates used as substrates in the biocatalytic process are also provided, as well as certain glycoconjugates.

Enzymatic synthesis of lipid II and analogues

The emergence of antibiotic resistance has prompted active research in the development of antibiotics with new modes of action. Among all essential bacterial proteins, transglycosylase polymerizes lipid II into peptidoglycan and is one of the most favorable targets because of its vital role in peptidoglycan synthesis. Described in this study is a practical enzymatic method for the synthesis of lipid II, coupled with cofactor regeneration, to give the product in a 50-70 % yield. This development depends on two key steps: the overexpression of MraY for the synthesis of lipid I and the use of undecaprenol kinase for the preparation of polyprenol phosphates. This method was further applied to the synthesis of lipid II analogues. It was found that MraY and undecaprenol kinase can accept a wide range of lipids containing various lengths and configurations. The activity of lipid II analogues for bacterial transglycolase was also evaluated.