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PMID:19560364
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| Citation |
Liu, XW, Xia, C, Li, L, Guan, WY, Pettit, N, Zhang, HC, Chen, M and Wang, PG (2009) Characterization and synthetic application of a novel beta1,3-galactosyltransferase from Escherichia coli O55:H7. Bioorg. Med. Chem. 17:4910-5 |
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| Abstract |
A beta1,3-galactosyltransferase (WbgO) was identified in Escherichia coli O55:H7. Its function was confirmed by radioactive activity assay and structure analysis of the disaccharide synthesized with the recombinant enzyme. WbgO requires a divalent metal ion, either Mn(2+) or Mg(2+), for its activity and is active between pH 6.0-8.0 with a pH optimum of 7.0. N-acetylglucosamine (GlcNAc) and oligosaccharides with GlcNAc at the non-reducing end were shown to be its preferred substrates and it can be used for the synthesis of type 1 glycan chains from these substrates. Together with a recombinant bacterial GlcNAc-transferase, benzyl beta-lacto-N-tetraoside was synthesized with the purified WbgO to demonstrate the synthetic utility of WbgO. |
| Links |
PubMed Online version:10.1016/j.bmc.2009.06.005 |
| Keywords |
Acetylglucosamine/metabolism; Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Galactosyltransferases/analysis; Galactosyltransferases/genetics; Galactosyltransferases/isolation & purification; Galactosyltransferases/metabolism; Magnesium/metabolism; Manganese/metabolism; Molecular Sequence Data; N-Acetylglucosaminyltransferases/genetics; N-Acetylglucosaminyltransferases/metabolism; Oligosaccharides/chemical synthesis; Oligosaccharides/chemistry; Oligosaccharides/metabolism; Recombinant Proteins/analysis; Recombinant Proteins/genetics; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Sequence Alignment; Substrate Specificity |
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