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This work reports the biochemical and functional analysis of the  Burkholderia cenocepacia  J2315  bceN  gene, encoding a protein with GDP-D-mannose 4,6-dehydratase enzyme activity (E.C.4.2.1.47). Data presented indicate that the protein is active when in the tetrameric form, catalyzing the conversion of GDP-D-mannose into GDP-4-keto-6-deoxy-D-mannose. This sugar nucleotide is the intermediary necessary for the biosynthesis of GDP-D-rhamnose, one of the sugar residues of cepacian, the major exopolysaccharide produced by environmental and human, animal and plant pathogenic isolates of the  Burkholderia cepacia  complex species. V max  and K m  values of 1.5±0.2 µmol.min −1 .mg −1  and 1024±123 µM, respectively, were obtained from the kinetic characterization of the  B. cenocepacia  J2315 BceN protein by NMR spectroscopy, at 25°C and in the presence of 1 mol MgCl 2  per mol of protein. The enzyme activity was strongly inhibited by the substrate, with an estimated K i  of 2913±350 µM. The lack of a functional  bceN  gene in a mutant derived from  B. cepacia  IST408 slightly reduced cepacian production. However, in the  B. multivorans  ATCC17616 with  bceN  as the single gene in its genome with predicted GMD activity, a  bceN  mutant did not produce cepacian, indicating that this gene product is required for cepacian biosynthesis.

Biochemical and Functional Studies on the Burkholderia cepacia Complex bceN Gene, Encoding a GDP-D-Mannose 4,6-Dehydratase