PubMed:26703456 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/26703456","sourcedb":"PubMed","sourceid":"26703456","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/26703456","text":"Biochemical characterization of an α1,2-colitosyltransferase from Escherichia coli O55:H7.\nColitose, also known as 3,6-dideoxy-l-galactose or 3-deoxy-l-fucose, is one of the only five naturally occurred 3,6-dideoxyhexoses. Colitose was found in lipopolysaccharide of a number of infectious bacteria, including Escherichia coli O55 \u0026 O111 and Vibrio cholera O22 \u0026 O139. To date, no colitosyltransferase (ColT) has been characterized, probably due to the inaccessibility of the sugar donor, GDP-colitose. In this study, starting with chemically prepared colitose, 94.6 mg of GDP-colitose was prepared via a facile and efficient one-pot two-enzyme system involving an l-fucokinase/GDP-l-Fuc pyrophosphorylase and an inorganic pyrophosphatase (EcPpA). WbgN, a putative ColT from E. coli O55:H5 was then cloned, overexpressed, purified and biochemically characterized by using GDP-colitose as a sugar donor. Activity assay and structural identification of the synthetic product clearly demonstrated that wbgN encodes an α1,2-ColT. Biophysical study showed that WbgN does not require metal ion, and is highly active at pH 7.5-9.0. In addition, acceptor specificity study indicated that WbgN exclusively recognize lacto-N-biose (Galβ1,3-GlcNAc). Most interestingly, it was found that WbgN exhibits similar activity toward GDP-l-Fuc (kcat/Km = 9.2 min(-1) mM(-1)) as that toward GDP-colitose (kcat/Km = 12 min(-1) mM(-1)). Finally, taking advantage of this, type 1 H-antigen was successfully synthesized in preparative 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