Identification of a UDP-Gal: GlcNAc-R galactosyltransferase activity in Escherichia coli VW187 |
| |
Authors: | Montoya-Peleaz Pedro J Riley John G Szarek Walter A Valvano Miguel A Schutzbach John S Brockhausen Inka |
| |
Affiliation: | Department of Chemistry, Queen's University, Kingston, Ontario, Canada K7L 3N6. |
| |
Abstract: | A novel acceptor substrate for galactosyltransferase was synthesized containing GlcNAcalpha-pyrophosphate, covalently bound to a hydrophobic phenoxyundecyl moiety (GlcNAc alpha-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. |
| |
Keywords: | |
本文献已被 ScienceDirect PubMed 等数据库收录! |