5.1.3.14 dihydropyrimidine-2,4(1H,3H)-dione-alpha-D-ribofuranosyl-5'-diphospho-2-acetamido-2-deoxy-alpha-D-mannopyranoside - Neisseria meningitidis serogroup A / serotype 4A ? - ? 445451 5.1.3.14 dihydropyrimidine-2,4(1H,3H)-dione-alpha-D-ribofuranosyl-5'-diphospho-2-acetamido-2-deoxy-alpha-D-mannopyranoside - Neisseria meningitidis serogroup A / serotype 4A Z2491 ? - ? 445451 5.1.3.14 additional information 3'-deoxy-UDP-N-acetylglucosamine is not a substrate Escherichia coli ? - ? 89 5.1.3.14 additional information bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase Rattus norvegicus ? - ? 89 5.1.3.14 additional information enzyme catalyzes the first step in synthesis of sialic acids Rattus norvegicus ? - ? 89 5.1.3.14 additional information reaction mechanism involving an anti-elimination of UDP to give 2-acetamidoglucal, followed by a syn-addition of water Rattus norvegicus ? - ? 89 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 Homo sapiens ? - ? 89 5.1.3.14 additional information key enzyme of N-acetylneuraminic acid biosynthesis Rattus norvegicus ? - ? 89 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 Homo sapiens ? - ? 89 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 Rattus norvegicus ? - ? 89 5.1.3.14 additional information the enzyme catalyzes the first step of sialic acid biosynthesis Rattus norvegicus ? - ? 89 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 Homo sapiens ? - ? 89 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 Homo sapiens ? - ? 89 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 Homo sapiens ? - ? 89 5.1.3.14 additional information biosynthesis of sialic acids Homo sapiens ? - ? 89 5.1.3.14 additional information biosynthesis of sialic acids Mus musculus ? - ? 89 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 Homo sapiens ? - ? 89 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 Mus musculus ? - ? 89 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 Homo sapiens ? - ? 89 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 Mus musculus ? - ? 89 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 Rattus norvegicus ? - ? 89 5.1.3.14 additional information GNE is a bifunctional enzyme with UDP-GlcNAc 2-epimerase and ManNAc kinase activities Mus musculus ? - ? 89 5.1.3.14 additional information GNE is a bifunctional enzyme with UDP-GlcNAc 2-epimerase and ManNAc kinase activities Homo sapiens ? - ? 89 5.1.3.14 additional information GNE is a bifunctional enzyme with UDP-GlcNAc 2-epimerase and ManNAc kinase activities Rattus norvegicus ? - ? 89 5.1.3.14 additional information substrate specificity, overview. Recombinant His6-tagged NmSacA-His6 can tolerate several chemoenzymatically synthesized UDP-ManNAc derivatives as substrates in the absence of UDP-GlcNAc although its activity is much lower than with non-modified UDP-ManNAc. Homology modeling and molecular docking. The formation of UDP-GlcNAc or UDP-ManNAc is not observed by incubating NmSacA-His6 with 2-acetamidoglucal and UDP in contrast to the serogroup B enzyme. No enzyme activity with UDP-mannose, UDP-ManF, UDP-ManN3, UDP-ManNH2, uridine 5'-diphospho-2-butyramido-2-deoxy-alpha-D-mannopyranoside, uridine 5'-diphospho-2-azidoacetamido-2-deoxy-alpha-D-mannopyranoside, uridine 5'-diphospho-2-phenylacetamido-2-deoxy-alpha-D-mannopyranoside, dihydropyrimidine-2, 4(1H,3H)-dione-alpha-D-ribofuranosyl-5'-diphospho-2-azidoxyacetamido-2-deoxy-alpha-D-mannopyranoside, and uridine 5'-diphospho-2-azidoacetamido-2-deoxy-alpha-D-glucopyranoside, docking study Neisseria meningitidis serogroup A / serotype 4A ? - ? 89 5.1.3.14 additional information the recombinnat enzyme His6-tagged NmSacA tolerates several chemoenzymatically synthesized UDP-ManNAc derivatives as substrates although its activity is much lower than with non-modified UDP-ManNAc, substrate specificity, overview Neisseria meningitidis serogroup A /serotype 4A ? - ? 89 5.1.3.14 additional information substrate specificity, overview. Recombinant His6-tagged NmSacA-His6 can tolerate several chemoenzymatically synthesized UDP-ManNAc derivatives as substrates in the absence of UDP-GlcNAc although its activity is much lower than with non-modified UDP-ManNAc. Homology modeling and molecular docking. The formation of UDP-GlcNAc or UDP-ManNAc is not observed by incubating NmSacA-His6 with 2-acetamidoglucal and UDP in contrast to the serogroup B enzyme. No enzyme activity with UDP-mannose, UDP-ManF, UDP-ManN3, UDP-ManNH2, uridine 5'-diphospho-2-butyramido-2-deoxy-alpha-D-mannopyranoside, uridine 5'-diphospho-2-azidoacetamido-2-deoxy-alpha-D-mannopyranoside, uridine 5'-diphospho-2-phenylacetamido-2-deoxy-alpha-D-mannopyranoside, dihydropyrimidine-2, 4(1H,3H)-dione-alpha-D-ribofuranosyl-5'-diphospho-2-azidoxyacetamido-2-deoxy-alpha-D-mannopyranoside, and uridine 5'-diphospho-2-azidoacetamido-2-deoxy-alpha-D-glucopyranoside, docking study Neisseria meningitidis serogroup A / serotype 4A Z2491 ? - ? 89 5.1.3.14 additional information the recombinnat enzyme His6-tagged NmSacA tolerates several chemoenzymatically synthesized UDP-ManNAc derivatives as substrates although its activity is much lower than with non-modified UDP-ManNAc, substrate specificity, overview Neisseria meningitidis serogroup A /serotype 4A Z2491 ? - ? 89 5.1.3.14 N-Acetyl-D-glucosamine - Rattus norvegicus ? - ? 925 5.1.3.14 N-Acetyl-D-glucosamine 1-phosphate - Rattus norvegicus ? - ? 926 5.1.3.14 UDP-GlcNAc biosynthesis of sialic acid Mus musculus ManNAc + UDP - ? 386738 5.1.3.14 UDP-GlcNAc biosynthetic pathway of sialic acid Escherichia coli ManNAc + UDP - ? 386738 5.1.3.14 UDP-GlcNAc sialic acid biosynthetic pathway Homo sapiens ManNAc + UDP - ? 386738 5.1.3.14 UDP-GlcNAc + H2O biosynthesis of sialic acids Rattus norvegicus ManNAc + UDP - ? 386735 5.1.3.14 UDP-glucose - Rattus norvegicus ? - ? 924 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine - Staphylococcus epidermidis UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine - Methanocaldococcus jannaschii UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine - Bacillus anthracis UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine - Staphylococcus aureus UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine - Neisseria meningitidis serogroup A / serotype 4A UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine - Bacillus subtilis UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine - Neisseria meningitidis serogroup A /serotype 4A UDP-N-acetyl-alpha-D-mannosamine - r 427566 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 Bacillus anthracis UDP-N-acetyl-alpha-D-mannosamine - r 427566 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 Staphylococcus aureus UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine interconversion Staphylococcus epidermidis UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine interconversion Staphylococcus aureus UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine interconversion Neisseria meningitidis serogroup A /serotype 4A UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine UDP-GlcNAc binding structure, overview Methanocaldococcus jannaschii UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine UDP-GlcNAc binding structure, overview Bacillus subtilis UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine - Bacillus subtilis 168 UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine UDP-GlcNAc binding structure, overview Bacillus subtilis 168 UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine - Neisseria meningitidis serogroup A / serotype 4A Z2491 UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine - Neisseria meningitidis serogroup A /serotype 4A Z2491 UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine interconversion Neisseria meningitidis serogroup A /serotype 4A Z2491 UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine - Staphylococcus aureus COL UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine interconversion Staphylococcus aureus COL UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine - Staphylococcus epidermidis CLB26329 UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine interconversion Staphylococcus epidermidis CLB26329 UDP-N-acetyl-alpha-D-mannosamine - r 427566 5.1.3.14 UDP-N-acetyl-alpha-D-mannosamine - Escherichia coli UDP-N-acetyl-alpha-D-glucosamine - r 445967 5.1.3.14 UDP-N-acetyl-alpha-D-mannosamine - Bacillus cereus UDP-N-acetyl-alpha-D-glucosamine - r 445967 5.1.3.14 UDP-N-acetyl-alpha-D-mannosamine - Neisseria meningitidis serogroup A / serotype 4A UDP-N-acetyl-alpha-D-glucosamine - r 445967 5.1.3.14 UDP-N-acetyl-alpha-D-mannosamine interconversion Staphylococcus epidermidis UDP-N-acetyl-alpha-D-glucosamine - r 445967 5.1.3.14 UDP-N-acetyl-alpha-D-mannosamine interconversion Staphylococcus aureus UDP-N-acetyl-alpha-D-glucosamine - r 445967 5.1.3.14 UDP-N-acetyl-alpha-D-mannosamine interconversion Neisseria meningitidis serogroup A /serotype 4A UDP-N-acetyl-alpha-D-glucosamine - r 445967 5.1.3.14 UDP-N-acetyl-alpha-D-mannosamine - Neisseria meningitidis serogroup A / serotype 4A Z2491 UDP-N-acetyl-alpha-D-glucosamine - r 445967 5.1.3.14 UDP-N-acetyl-alpha-D-mannosamine interconversion Neisseria meningitidis serogroup A /serotype 4A Z2491 UDP-N-acetyl-alpha-D-glucosamine - r 445967 5.1.3.14 UDP-N-acetyl-alpha-D-mannosamine interconversion Staphylococcus aureus COL UDP-N-acetyl-alpha-D-glucosamine - r 445967 5.1.3.14 UDP-N-acetyl-alpha-D-mannosamine interconversion Staphylococcus epidermidis CLB26329 UDP-N-acetyl-alpha-D-glucosamine - r 445967 5.1.3.14 UDP-N-acetyl-D-glucosamine - Bacillus subtilis UDP-N-acetyl-D-mannosamine - ? 923 5.1.3.14 UDP-N-acetyl-D-glucosamine - Escherichia coli UDP-N-acetyl-D-mannosamine - ? 923 5.1.3.14 UDP-N-acetyl-D-glucosamine - Escherichia coli UDP-N-acetyl-D-mannosamine - r 923 5.1.3.14 UDP-N-acetyl-D-glucosamine - Homo sapiens UDP-N-acetyl-D-mannosamine - ? 923 5.1.3.14 UDP-N-acetyl-D-glucosamine - Rattus norvegicus UDP-N-acetyl-D-mannosamine - ? 923 5.1.3.14 UDP-N-acetyl-D-glucosamine - Priestia megaterium UDP-N-acetyl-D-mannosamine - ? 923 5.1.3.14 UDP-N-acetyl-D-glucosamine - Methanococcus maripaludis UDP-N-acetyl-D-mannosamine - r 923 5.1.3.14 UDP-N-acetyl-D-glucosamine r Escherichia coli UDP-N-acetyl-D-mannosamine - ? 923 5.1.3.14 UDP-N-acetyl-D-glucosamine the reverse reaction with UDP-N-acetylmannosamine requires the presence of UDP-N-acetylglucosamine Escherichia coli UDP-N-acetyl-D-mannosamine - ? 923 5.1.3.14 UDP-N-acetyl-D-glucosamine the reverse reaction with UDP-N-acetylmannosamine requires the presence of UDP-N-acetylglucosamine Bacillus cereus UDP-N-acetyl-D-mannosamine - ? 923 5.1.3.14 UDP-N-acetyl-D-glucosamine reversibility is not detected Rattus norvegicus UDP-N-acetyl-D-mannosamine - ? 923 5.1.3.14 UDP-N-acetyl-D-glucosamine first step of sialic acid biosynthesis Neisseria meningitidis UDP-N-acetyl-D-mannosamine - ? 923 5.1.3.14 UDP-N-acetyl-D-glucosamine key enzyme of sialic acid biosynthesis Rattus norvegicus UDP-N-acetyl-D-mannosamine - ? 923 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 Homo sapiens UDP-N-acetyl-D-mannosamine - ? 923 5.1.3.14 UDP-N-acetyl-D-glucosamine characterization of ligand binding to the bifunctional enzyme Rattus norvegicus UDP-N-acetyl-D-mannosamine - ? 923 5.1.3.14 UDP-N-acetyl-D-glucosamine mechanism involves an anti elimination of UDP to form 2-acetamidoglucal as an intermediate, followed by syn-addition of water Neisseria meningitidis UDP-N-acetyl-D-mannosamine - ? 923 5.1.3.14 UDP-N-acetyl-D-glucosamine non-hydrolizing Bacillus anthracis UDP-N-acetyl-D-mannosamine - ? 923 5.1.3.14 UDP-N-acetyl-D-glucosamine first step of sialic acid biosynthesis Neisseria meningitidis MC58 group B UDP-N-acetyl-D-mannosamine - ? 923 5.1.3.14 UDP-N-acetyl-D-glucosamine mechanism involves an anti elimination of UDP to form 2-acetamidoglucal as an intermediate, followed by syn-addition of water Neisseria meningitidis MC58 group B UDP-N-acetyl-D-mannosamine - ? 923 5.1.3.14 UDP-N-acetyl-D-glucosamine - Rattus norvegicus ? - ? 369253 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 Escherichia coli ? - ? 369253 5.1.3.14 UDP-N-acetyl-D-glucosamine enzyme of the N-acetylneuraminic acid metabolic pathway Homo sapiens ? - ? 369253 5.1.3.14 UDP-N-acetyl-D-glucosamine enzyme of biosynthesis of N-acetylneuraminic acid Rattus norvegicus ? - ? 369253 5.1.3.14 UDP-N-acetyl-D-glucosamine initial enzyme responsible for the biosynthesis of CMP-N-acetylneuraminic acid Rattus norvegicus ? - ? 369253 5.1.3.14 UDP-N-acetyl-D-glucosamine possible role in the biogenesis of N-acetylmannosamine-containing macromolecules Rattus norvegicus ? - ? 369253 5.1.3.14 UDP-N-acetyl-D-glucosamine - Rattus norvegicus Wistar ? - ? 369253 5.1.3.14 UDP-N-acetyl-D-glucosamine + H2O - Mus musculus UDP + N-acetylmannosamine - ? 407444 5.1.3.14 UDP-N-acetyl-D-glucosamine + H2O - Homo sapiens UDP + N-acetylmannosamine - ? 407444 5.1.3.14 UDP-N-acetyl-D-glucosamine + H2O - Rattus norvegicus UDP + N-acetylmannosamine - ? 407444 5.1.3.14 UDP-N-acetyl-D-glucosamine + H2O epimerase active site amino acid residues D21, G111, H132, G136 and D144 are required for stabilization of the active site structure, residues R19, S301 and E307 are involved in binding of the UDP portion of the substrate. Amino acid residues K24, P27, M29, D112, E134, D143, D144, R147, S302 and R113 are located in vicinity of the active site, while residues G182 and D187 are part of the active site hinge region. The possible general catalyst is residue H220, and residues H45 and H132 are required for 2-epimerase activity Homo sapiens UDP + N-acetylmannosamine - ? 407444 5.1.3.14 UDP-N-acetylgalactosamine - Rattus norvegicus ? - ? 927 5.1.3.14 uridine 5'-diphospho-2-hydroxyacetamido-2-deoxy-alpha-D-mannopyranoside - Neisseria meningitidis serogroup A / serotype 4A ? - ? 445970 5.1.3.14 uridine 5'-diphospho-2-hydroxyacetamido-2-deoxy-alpha-D-mannopyranoside - Neisseria meningitidis serogroup A / serotype 4A Z2491 ? - ? 445970 5.1.3.14 uridine 5'-diphospho-2-propionamido-2-deoxy-alpha-D-mannopyranoside - Neisseria meningitidis serogroup A / serotype 4A ? - ? 445971 5.1.3.14 uridine 5'-diphospho-N-trifluoroaceto-2-deoxy-alpha-D-mannopyranoside - Neisseria meningitidis serogroup A / serotype 4A ? - ? 445972