ThesiaAgene involved in capsule polysaccharide biosynthesis ofNeisseria meningitidisB codes forN-acylglucosamine-6-phosphate 2-epimerase activity
Open Access
- 1 March 2000
- journal article
- Published by Oxford University Press (OUP) in FEMS Microbiology Letters
- Vol. 184 (2) , 161-164
- https://doi.org/10.1111/j.1574-6968.2000.tb09008.x
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.Keywords
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