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Michael Petersen, Wolf-Dieter Fessner, Matthias Frosch, Edeltraud Lüneberg, The siaA gene involved in capsule polysaccharide biosynthesis of Neisseria meningitidis B codes for N-acylglucosamine-6-phosphate 2-epimerase activity, FEMS Microbiology Letters, Volume 184, Issue 2, March 2000, Pages 161–164, https://doi.org/10.1111/j.1574-6968.2000.tb09008.x
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Abstract
The capsule polysaccharide of Neisseria meningitidis serogroup B is composed of a homopolymer of α-2→8 linked N-acetyl-neuraminic acid (sialic acid). The enzymes required for sialic acid biosynthesis and polymerization are encoded in region A of the capsule gene complex. We here describe the enzymatic activity of the siaA gene product as determined by biochemical analysis. siaA was overexpressed in Escherichia coli and the SiaA protein was purified to homogeneity. Enzymatic assays revealed that SiaA did not accept N-acetyl-glucosamine as substrate, but only N-acetyl-glucosamine-6-phosphate (EC 5.1.3.9). SiaA catalyzes the isomerization of N-acetyl-glucosamine-6-phosphate to form N-acetyl-mannosamine-6-phosphate. This reaction represents the first step in capsule biosynthesis of N. meningitidis B.