Collect. Czech. Chem. Commun. 2004, 69, 1829-1842

Inhibition of Biosynthesis and Biochemical Modulation of N-Acylneuraminic Acid (Biochemical Engineering of Sialoconjugates). A Review

Werner Reutter* and Rüdiger Horstkorte

Institut für Biochemie und Molekularbiologie, Charité - Universitätsmedizin Berlin, Campus Benjamin Franklin, Arnimallee 22, 14195 Berlin-Dahlem, Germany


The key enzyme of sialic acid biosynthesis is the bifunctional UDP-GlcNAc 2-epimerase/ ManNAc kinase. Novel inhibitors of this enzyme have been synthesized. The N-acyl side chain of sialic acid can be biochemically engineered by incubating cells with non-natural N-acylmannosamine analogues such as N-propionylmannosamine and related compounds. These modified sialic acids lead to various biological changes, such as stimulation of T-lymphocyte proliferation, inhibition of the uptake of influenza A virus, stimulation of neuritic growth, increased expression of sialyl-Lewisx and altered adhesion. A review with 41 references.

Keywords: UDP-N-acetylglucosamine 2-epimerase/N-acylmannosamine kinase inhibitors; N-Acetylneuraminic acid; N-Propionylneuraminic acid; N-Propionylmannosamine; Influenza viruses; T-lymphocytes; Neurite growth; Sialyl-Lewisx; Recombinant glycoproteins; Glycans; Sialic acid; Sialylation.

References: 41 live references.