Abstract
A novel acceptor substrate for galactosyltransferase was synthesized containing GlcNAcα-pyrophosphate, covalently bound to a hydrophobic phenoxyundecyl moiety (GlcNAc α-O-PO 3-PO 3-(CH 2) 11-O-Phenyl). The new substrate was used to develop an assay for a galactosyltransferase activity from Escherichia coli strain VW187 that is involved in lipopolysaccharide synthesis and has not been studied by others. We showed that Gal was transferred from UDP-Gal to the novel acceptor substrate. This was a significant improvement over our previous preliminary assays of the enzyme using endogenous substrate, and showed that these synthetic substrates are useful for assaying enzymes that utilize lipid-bound substrates in O-chain synthesis in Gram-negative bacteria.
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