From peptidoglycan to glycoproteins: common features of lipid-linked oligosaccharide biosynthesis.
The peptidoglycan layer of bacterial cell walls is biosynthesised using a lipid carrier undecaprenyl phosphate to assemble and transport the MurNAc(GlcNAc)-pentapeptide precursor. Similar lipid-linked cycles are involved in the biosynthesis of other bacterial exopolysaccharides and eukaryotic asparagine-linked glycoproteins, the latter involving the structurally related dolichyl phosphate as a lipid carrier. Recent protein sequence data and common inhibitors of the bacterial and eukaryotic systems have revealed functional similarities between the two systems. Biological and physical studies on the lipid carriers themselves have provided clues to their role in oligosaccharide translocation, but have not revealed significant differences in function between undecaprenyl phosphate and dolichyl phosphate. The presence of dolichyl phosphate and a family of saturated isoprenoid lipids in Archaebacteria suggests a possible evolutionary link between the two systems.
Bugg
T D
TD
Department of Chemistry, University of Southampton, Highfield, UK.
Brandish
P E
PE
D000595:Amino Acid Sequence; D001419:Bacteria / Q000378:metabolism*; D004288:Dolichol Phosphates / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000096:biosynthesis*; D008969:Molecular Sequence Data; D010457:Peptidoglycan / Q000096:biosynthesis*; D011106:Polyisoprenyl Phosphates / Q000378:metabolism*
D004288:Dolichol Phosphates; D008562:Membrane Glycoproteins; D010457:Peptidoglycan; D011106:Polyisoprenyl Phosphates; C028306:dolichol monophosphate; C009621:undecaprenyl phosphate