{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Pettit N"],"funding":["NICHD NIH HHS","US National Institutes of Child Health & Human Development","US National Institutes of Genetic Medical Sciences","NIGMS NIH HHS"],"pagination":["190-5"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3441828"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["402(2)"],"pubmed_abstract":["Escherichia coli O127:K63(B8) possesses high human blood group H (O) activity due to its O-antigen repeating unit structure. In this work, the wbiQ gene from E. coli O127:K63(B8) was expressed in E. coli BL21 (DE3) and purified as a fusion protein containing an N-terminal GST affinity tag. Using the GST-WbiQ fusion protein, the wbiQ gene was identified to encode an α1,2-fucosyltransferase using a radioactivity based assay, thin-layer chromatography assay, as well confirming product formation by using mass spectrometry and NMR spectroscopy. The fused enzyme (GST-WbiQ) has an optimal pH range from 6.5 to 7.5 and does not require the presence of a divalent metal to be enzymatically active. WbiQ displays strict substrate specificity, displaying activity only towards acceptors that contain Gal-"],"journal":["Biochemical and biophysical research communications"],"pubmed_title":["Characterization of WbiQ: An α1,2-fucosyltransferase from Escherichia coli O127:K63(B8), and synthesis of H-type 3 blood group antigen."],"pmcid":["PMC3441828"],"funding_grant_id":["R01 HD061935","R01 GM085267"],"pubmed_authors":["Wang PG","Pettit N","Mei Z","Han W","Zhao G","Styslinger T"],"additional_accession":[]},"is_claimable":false,"name":"Characterization of WbiQ: An α1,2-fucosyltransferase from Escherichia coli O127:K63(B8), and synthesis of H-type 3 blood group antigen.","description":"Escherichia coli O127:K63(B8) possesses high human blood group H (O) activity due to its O-antigen repeating unit structure. In this work, the wbiQ gene from E. coli O127:K63(B8) was expressed in E. coli BL21 (DE3) and purified as a fusion protein containing an N-terminal GST affinity tag. Using the GST-WbiQ fusion protein, the wbiQ gene was identified to encode an α1,2-fucosyltransferase using a radioactivity based assay, thin-layer chromatography assay, as well confirming product formation by using mass spectrometry and NMR spectroscopy. The fused enzyme (GST-WbiQ) has an optimal pH range from 6.5 to 7.5 and does not require the presence of a divalent metal to be enzymatically active. WbiQ displays strict substrate specificity, displaying activity only towards acceptors that contain Gal-","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Nov","modification":"2026-05-04T20:46:06.613Z","creation":"2019-03-27T00:57:56Z"},"accession":"S-EPMC3441828","cross_references":{"pubmed":["20801103"],"doi":["10.1016/j.bbrc.2010.08.087"]}}