Publication | Open Access
Acyl-acyl carrier protein specificity of UDP-GlcNAc acyltransferases from gram-negative bacteria: relationship to lipid A structure
65
Citations
26
References
1991
Year
Bioorganic ChemistryBacteriologyGlycobiologyPolysaccharideUdp-glcnac AcyltransferasesLipid ABiosynthesisFatty AcidsMetabolic EngineeringMembrane AnchorGlycosylationBiochemistryGram-negative BacteriaMolecular MicrobiologyGram-negative BacteriologyNatural SciencesMicrobiologyMedicineCarbohydrate-protein Interaction
Lipid A, the component of lipopolysaccharide that provides the membrane anchor of the core and O-antigen sugars, is known to contain characteristic R-3-hydroxy fatty acids bound to the 2,2' (N-linked) and 3,3' (O-linked) positions of the glucosamine disaccharide in different gram-negative bacteria. The studies reported here show that it is the acyl-acyl carrier protein specificities of the enzymes UDP-GlcNAc-O-acyltransferase and UDP-3-O-[(R)-3-hydroxyacyl]-GlcN-N-acyltransferase that determine the nature of these fatty acids.
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