5.1.3.14 additional information key enzyme for biosynthesis of N-acetylneuraminate is the bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, catalyzing the first two steps of the biosynthesis in the cytosol 5.1.3.14 additional information key enzyme of N-acetylneuraminic acid biosynthesis 5.1.3.14 additional information rate-limiting step in sialic acid biosynthesis pathway. The enzyme is the major determinant of cell surface sialylation in hematopoietic cell lines and is a critical regulator of the function of specific cell surface adhesion molecules 5.1.3.14 additional information the bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/ManNAc kinase catalyzes the first two steps in the biosynthesis of the sialic acids 5.1.3.14 additional information the enzyme catalyzes the first step of sialic acid biosynthesis 5.1.3.14 additional information downregulation of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase in hyposialylated HIV-infected T cells with consequential glycosylation modification (the deficiency can be entirely corrected by nutrient complementation with N-acetylmannosamine). The promoter of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase is de novo hypermethylated in HIV-infected CEM cells 5.1.3.14 additional information the bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase is a rate-limiting enzyme of sialic acid biosynthesis 5.1.3.14 additional information the homozygous M712T mutation of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase results in reduced enzyme activities but not in altered overall cellular sialylation in hereditary inclusion body myopathy 5.1.3.14 additional information biosynthesis of sialic acids 5.1.3.14 additional information role of splice variant GNE1 in basic supply of cells with sialic acids, whereas GNE2 and GNE3 may have a function in finetuning of the sialic acid pathway 5.1.3.14 additional information role of splice variant GNE1 in basic supply of cells with sialic acids, whereas GNE2 and GNE3 may have a function in finetuning of the sialic acid pathway. No significant differences in activities of splice variants mGNE 1 and mGNE2 5.1.3.14 additional information GNE interacts with proteins involved in the regulation of development, e.g. the transcription factor promyelotic leukemia zinc finger protein, which might play a crucial role in the hereditary inclusion body myopathy. GNE is regulated by a variety of biochemical means, including tetramerization promoted by the substrate UDP-GlcNAc, phosphorylation by protein kinase C and feedback inhibition by CMP-Neu5Ac, which is defect in the human disease sialuria. Multienzyme complexes of GNE with the other enzymes of the sialic acid biosynthesis pathway, either close to the Golgi CMP sialic acid transporter or in particular with the nuclear localized CMP-sialic acid synthetase, are possible 5.1.3.14 additional information GNE interacts with proteins involved in the regulation of development, e.g. the transcription factor promyelotic leukemia zinc finger protein, which might play a crucial role in the hereditary inclusion body myopathy. GNE is regulated by a variety of biochemical means, including tetramerization promoted by the substrate UDP-GlcNAc, phosphorylation by protein kinase C and feedback inhibition by CMP-Neu5Ac. Multienzyme complexes of GNE with the other enzymes of the sialic acid biosynthesis pathway, either close to the Golgi CMP sialic acid transporter or in particular with the nuclear localized CMP-sialic acid synthetase, are possible 5.1.3.14 UDP-GlcNAc biosynthesis of sialic acid 5.1.3.14 UDP-GlcNAc biosynthetic pathway of sialic acid 5.1.3.14 UDP-GlcNAc sialic acid biosynthetic pathway 5.1.3.14 UDP-GlcNAc + H2O biosynthesis of sialic acids 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine - 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine allosteric regulatory mechanism, which involves direct interaction between one substrate molecule in the active site and another in the allosteric site 5.1.3.14 UDP-N-acetyl-D-glucosamine first step of sialic acid biosynthesis 5.1.3.14 UDP-N-acetyl-D-glucosamine key enzyme of sialic acid biosynthesis 5.1.3.14 UDP-N-acetyl-D-glucosamine reduction of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase activity and sialylation in distal myopathy with rimmed vacuoles 5.1.3.14 UDP-N-acetyl-D-glucosamine - 5.1.3.14 UDP-N-acetyl-D-glucosamine UDP-N-acetyl-D-glucosamine 2-epimerase and UDP-N-acetyl-D-mannosamine dehydrogenase are responsible for the formation of UDP-N-acetyl-D-mannosaminuronic acid from UDP-N-acetyl-D-glucosamine 5.1.3.14 UDP-N-acetyl-D-glucosamine enzyme of the N-acetylneuraminic acid metabolic pathway 5.1.3.14 UDP-N-acetyl-D-glucosamine enzyme of biosynthesis of N-acetylneuraminic acid 5.1.3.14 UDP-N-acetyl-D-glucosamine initial enzyme responsible for the biosynthesis of CMP-N-acetylneuraminic acid 5.1.3.14 UDP-N-acetyl-D-glucosamine possible role in the biogenesis of N-acetylmannosamine-containing macromolecules 5.1.3.14 UDP-N-acetyl-D-glucosamine + H2O -