Phytanyl-pyrophosphate-linked substrate for a bacterial alpha-mannosyltransferase

Biochem Biophys Res Commun. 2000 May 27;272(1):290-2. doi: 10.1006/bbrc.2000.2771.


The biochemical characterization of bacterial glycosyltransferases involved in the assembly of cell-wall-associated polysaccharides is often hindered by the lack of the appropriate undecaprenyl-pyrophosphate-linked acceptor substrate. In order to find a suitable synthetic substrate for the alpha1,3-mannosyltransferase AceA from Acetobacter xylinum, phytanyl-pyrophosphate-linked cellobiose was prepared. In the presence of GDP-[14C]mannose and recombinant AceA, the phytanyl-pyrophosphate-linked cellobiose afforded a 14C-labeled trisaccharide that was sensitive to alpha-mannosidase degradation in a fashion analogous to the natural undecaprenyl-pyrophosphate-linked cellobiose substrate. These results suggest that phytanyl-pyrophosphate-linked oligosaccharides may be useful substrates for other important bacterial glycosyltransferases.

MeSH terms

  • Acetobacter / enzymology
  • Cellobiose / chemistry
  • Cellobiose / metabolism
  • Mannosyltransferases / metabolism*
  • Molecular Structure
  • Polyisoprenyl Phosphate Oligosaccharides / chemistry
  • Polyisoprenyl Phosphate Oligosaccharides / metabolism
  • Recombinant Proteins / metabolism
  • Substrate Specificity


  • Polyisoprenyl Phosphate Oligosaccharides
  • Recombinant Proteins
  • Cellobiose
  • GDP-mannose - cellobiosyl-diphosphopolyprenol mannosyltransferase
  • Mannosyltransferases