The enzyme participates in the biosynthesis of the sialic acid 3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonate (Kdn). The human sialic acid synthase (EC 2.5.1.57) is also able to catalyse the reaction. Kdn is abundant in extracellular glycoconjugates of lower vertebrates such as fish and amphibians, but is also found in the capsular polysaccharides of bacteria that belong to the Bacteroides genus.
The enzyme participates in the biosynthesis of the sialic acid 3-deoxy-D-glycero-D-galacto-non-2-ulopyranosonate (Kdn). The human sialic acid synthase (EC 2.5.1.57) is also able to catalyse the reaction. Kdn is abundant in extracellular glycoconjugates of lower vertebrates such as fish and amphibians, but is also found in the capsular polysaccharides of bacteria that belong to the Bacteroides genus.
the enzyme prefers N-acetyl-D-mannose 6-phosphate over D-mannose 6-phosphate in the production of phosphorylated forms of N-acetylneuraminic acid and 2-dehydro-3-deoxy-D-glycero-D-galacto-nononic acid
the 3-deoxy-D-glycero-D-galacto-nononate unit might be used to protect the cell from bacteriophage invasion and/or to mimic the human epithelial cell surface
the enzyme prefers N-acetyl-D-mannose 6-phosphate over D-mannose 6-phosphate in the production of phosphorylated forms of N-acetylneuraminic acid and 2-dehydro-3-deoxy-D-glycero-D-galacto-nononic acid
the 3-deoxy-D-glycero-D-galacto-nononate unit might be used to protect the cell from bacteriophage invasion and/or to mimic the human epithelial cell surface
the enzyme is active in the absence of exogenously added divalent cations but lost all activity when incubated before assay with 5 mM EDTA. The lost enzyme activity is restored to 2.43 times higher levels of the original one by the addition of 1 mM MnCl2, CoCl2, or NiCl2 and to one-third the original activity by 1 mM MgCl2. The other cations (Ca2+, Fe2+, Cu2+, and Zn2+) do not restore enzyme activity
the M42L mutant of N-acetylneuraminic acid-9-phosphate synthase, like the wild type enzyme, shows the additional 2-keto-3-deoxy-D-glycero-D-galacto-nonulosonic acid-9-phosphate synthase activity
the mutation of N-acetylneuraminic acid-9-phosphate synthase abolishes its 2-keto-3-deoxy-D-glycero-D-galacto-nonulosonic acid-9-phosphate synthase activity
the mutant of N-acetylneuraminic acid-9-phosphate synthase has significant 2-keto-3-deoxy-D-glycero-D-galacto-nonulosonic acid-9-phosphate synthase activity
replacement of the antifreeze-like domain of human N-acetylneuraminic acid phosphate synthase with the mouse antifreeze-like domain impacts both N-acetylneuraminic acid 9-phosphate synthase and 2-keto-3-deoxy-D-glycero-D-galacto-nonulosonic acid 9-phosphate synthase activities
the gene partially restores sialic acid synthase activity in a neuB-negative mutant of Escherichia coli and results in N-acetylneuraminic acid (Neu5Ac) and 2-dehydro-3-deoxy-D-glycero-D-galacto-nononic acid production in insect cells upon recombinant baculovirus infection
Hao, J.; Vann, W.F.; Hinderlich, S.; Sundaramoorthy, M.
Elimination of 2-keto-3-deoxy-D-glycero-D-galacto-nonulosonic acid 9-phosphate synthase activity from human N-acetylneuraminic acid 9-phosphate synthase by a single mutation
Replacement of the antifreeze-like domain of human N-acetylneuraminic acid phosphate synthase with the mouse antifreeze-like domain impacts both N-acetylneuraminic acid 9-phosphate synthase and 2-keto-3-deoxy-D-glycero-D-galacto-nonulosonic acid 9-phosphate synthase activities
Biosynthesis of KDN (2-keto-3-deoxy-D-glycero-D-galacto-nononic acid). Identification and characterization of a KDN-9-phosphate synthetase activity from trout testis
Cloning and expression of the human N-acetylneuraminic acid phosphate synthase gene with 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid biosynthetic ability