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ATP + D-glucose
ADP + D-glucose 6-phosphate
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine-6-phosphate
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
ATP + N-glycolylmannosamine
N-glycolylmannosamine-6-phosphate
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Substrates: -
Products: -
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additional information
?
-
ATP + D-glucose
ADP + D-glucose 6-phosphate
Substrates: -
Products: -
r
ATP + D-glucose
ADP + D-glucose 6-phosphate
Substrates: -
Products: -
r
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
Substrates: -
Products: -
r
ATP + N-acetyl-D-glucosamine
ADP + N-acetyl-D-glucosamine 6-phosphate
Substrates: -
Products: -
r
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: involved in N-acetylneuraminic acid metabolism, key enzyme in N-acetylneuraminic acid biosynthesis
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: metabolic pathway between hexoses and sialic acids
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: enzyme is involved in sialic acid metabolism
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: enzyme is involved in sialic acid metabolism
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: involved in N-acetylneuraminic acid metabolism, key enzyme in N-acetylneuraminic acid biosynthesis
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: highly specific for ATP and N-acetyl-D-mannosamine
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
Substrates: -
Products: -
r
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
Substrates: -
Products: -
r
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine-6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine-6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine-6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine-6-phosphate
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine-6-phosphate
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine-6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine-6-phosphate
-
Substrates: -
Products: -
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ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine-6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine-6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine-6-phosphate
-
Substrates: highly specific for ATP and N-acetyl-D-mannosamine
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine-6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
Substrates: -
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
Substrates: -
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
Substrates: -
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
Substrates: -
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
Substrates: key and rate limiting enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids, enzyme mutations can cause hereditary inclusion body myopathy
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
Substrates: key enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids, essential for early embryonic development, enzyme involved in several genetic disorders such as sialuria, hereditary inclusion body myopathy, and Nonaka myopathy
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
Substrates: key enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids, mutations in the enzyme causes hereditary inclusion body myopathy
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
Substrates: key enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids, reduced activity causes distal myopathy with rimmed vacuoles
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
Substrates: key enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids, essential for early embryonic development
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
Substrates: key enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
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additional information
?
-
Substrates: UDP-GlcNAc 2-epimerase and ManNAc kinase are parts of one bifunctional enzyme, catalyzes the first 2 steps in N-acetylneuraminic acid biosynthesis
Products: -
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additional information
?
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Substrates: isoform GNE2 displays an extended N-terminus compared with isoform GNE, which is linked directly to the epimerase domain. Recombinant GNE2 still possesses both enzymatic activities of GNE
Products: -
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additional information
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Substrates: isoform GNE3 displays an deleted N-terminus compared with isoform GNE. Recombinant GNE3 shows a total loss of the epimerase activity
Products: -
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additional information
?
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Substrates: the enzyme is a bifunctional enzyme uridine diphosphate 1-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, i.e. UDP-GlcNAc 2-epimerase/ManNAc kinase or GNE. The N-terminal domain carries out UDP-GlcNAc epimerase function, whereas the C-terminal domain is responsible for ManNAc kinase activity
Products: -
?
additional information
?
-
Substrates: UDP-GlcNAc 2-epimerase and ManNAc kinase are parts of one bifunctional enzyme, catalyzes the first 2 steps in N-acetylneuraminic acid biosynthesis
Products: -
?
additional information
?
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-
Substrates: displays N-acetylglucosamine kinase activity as well as N-acetylmannosamine kinase activity
Products: -
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additional information
?
-
Substrates: UDP-GlcNAc 2-epimerase and ManNAc kinase are parts of one bifunctional enzyme, catalyzes the first 2 steps in N-acetylneuraminic acid biosynthesis
Products: -
?
additional information
?
-
-
Substrates: D-glucose, D-mannose, N-acetyl-D-glucosamine and N-acetyl-D-galactosamine are not phosphorylated
Products: -
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additional information
?
-
-
Substrates: N-acetylglucosamine and N-glycolylglucosamine, N-acetylgalactosamine, mannosamine, glucosamine, galactosamine, mannose, galactose, fructose, glucose, glucose-1-phosphate and glucose-6-phosphate are inactive as substrates, the phosphoryl donor ATP cannot be replaced by GTP, UTP, CTP, TTP, dATP or phosphoenolpyruvate
Products: -
?
additional information
?
-
-
Substrates: UDP-GlcNAc 2-epimerase and ManNAc kinase are parts of one bifunctional enzyme, catalyzes the first 2 steps in N-acetylneuraminic acid biosynthesis
Products: -
?
additional information
?
-
-
Substrates: UDP-GlcNAc 2-epimerase and ManNAc kinase are parts of one bifunctional enzyme, catalyzes the first 2 steps in N-acetylneuraminic acid biosynthesis
Products: -
?
additional information
?
-
-
Substrates: UDP-GlcNAc 2-epimerase and ManNAc kinase are parts of one bifunctional enzyme, catalyzes the first 2 steps in N-acetylneuraminic acid biosynthesis
Products: -
?
additional information
?
-
-
Substrates: UDP-GlcNAc 2-epimerase and ManNAc kinase are parts of one bifunctional enzyme, catalyzes the first 2 steps in N-acetylneuraminic acid biosynthesis
Products: -
?
additional information
?
-
-
Substrates: UDP-GlcNAc 2-epimerase and ManNAc kinase are parts of one bifunctional enzyme, catalyzes the first 2 steps in N-acetylneuraminic acid biosynthesis
Products: -
?
additional information
?
-
-
Substrates: glucose, mannose, fructose, glucosamine, N-acetylglucosamine and N-acetylgalactosamine are inactive as substrates
Products: -
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additional information
?
-
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Substrates: no enzyme found when bacteria grow in presence of glucose
Products: -
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ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
additional information
?
-
Substrates: the enzyme is a bifunctional enzyme uridine diphosphate 1-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, i.e. UDP-GlcNAc 2-epimerase/ManNAc kinase or GNE. The N-terminal domain carries out UDP-GlcNAc epimerase function, whereas the C-terminal domain is responsible for ManNAc kinase activity
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
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ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
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ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: involved in N-acetylneuraminic acid metabolism, key enzyme in N-acetylneuraminic acid biosynthesis
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: metabolic pathway between hexoses and sialic acids
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: enzyme is involved in sialic acid metabolism
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: enzyme is involved in sialic acid metabolism
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: involved in N-acetylneuraminic acid metabolism, key enzyme in N-acetylneuraminic acid biosynthesis
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
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ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: highly specific for ATP and N-acetyl-D-mannosamine
Products: -
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
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ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
Substrates: -
Products: -
r
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
Substrates: -
Products: -
r
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
Substrates: -
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
Substrates: -
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
Substrates: -
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
Substrates: -
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
Substrates: key and rate limiting enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids, enzyme mutations can cause hereditary inclusion body myopathy
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
Substrates: key enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids, essential for early embryonic development, enzyme involved in several genetic disorders such as sialuria, hereditary inclusion body myopathy, and Nonaka myopathy
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
Substrates: key enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids, mutations in the enzyme causes hereditary inclusion body myopathy
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
Substrates: key enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids, reduced activity causes distal myopathy with rimmed vacuoles
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
Substrates: key enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids, essential for early embryonic development
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
Substrates: key enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids
Products: -
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
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ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
Substrates: -
Products: -
?
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evolution
sequence comparion and modeling of human hGNE1 and mouse mGne1 isozymmess, overview
evolution
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sequence comparion and modeling of human hGNE1 and mouse mGne1 isozymmess, overview
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malfunction
all cases of hereditary inclusion body myopathy and distal myopathy with rimmed vacuoles are caused by mutations
malfunction
mutations cause sialurea or inclusion body myopathy/Nonaka myopathy
malfunction
enzyme mutations can cause sialuria and hereditary inclusion body myopathy. Sialuria patients have a heterozygous missense mutation affecting the allosteric site of GNE, leading to loss of feedback inhibition of GNE-epimerase activity by CMP-Neu5Ac, resulting in excessive sialic acid production. HIBM and its allelic Japanese disorder, distal myopathy with rimmed vacuoles, or DMRV, is an autosomal recessive neuromuscular disorder of adult onset, characterized byslowly progressive muscle weakness and atrophy
malfunction
heterozygous UDP-GlcNAc 2-epimerase and N-acetylmannosamine kinase domain mutations in the GNE gene result in a less severe GNE myopathy phenotype compared to homozygous N-acetylmannosamine kinase domain mutations, screening study of mutant individuals, genotypes of the GNE myopathy patient population and phenotypes, overview
malfunction
non-allosteric GNE gene mutations cause the muscular disorder GNE myopathy, i.e. hereditary inclusion body myopathy. Complete Gne knockout is embryonically lethal. Transgenic mice expressing the human GNE cDNA with the D176V mutation, common among Japanese patients, in a mouse background with a disrupted mouse Gne gene recapitulates the adult onset features of human GNE myopathy with hyposialylation in serum and different organs. M712T mouse mutants die within 72 h of birth from severe glomerular disease. Mouse isozyme mutant phenotypes, overview
malfunction
silencing of GNE sensitizes pancreatic cancer cells to anoikis, an apoptosis program activated on loss of matrix anchorage. A loss of GNE enzyme activity in cells renders them anoikis-susceptible after transfection with the tumor suppressor p16. ManNAc incubation reduces anoikis susceptibility, phenotype, overview. Enzyme up-regulation occurs predominantly in pancreatic cancer but also in other malignancies
malfunction
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stable knock-down of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase in HEK-293 cells dramatically increases incorporation of N-acetylmannosamine analogues into glycoproteins of HEK-293 cells
malfunction
enzyme mutation affects beta1-integrin-mediated cell adhesion process
malfunction
-
non-allosteric GNE gene mutations cause the muscular disorder GNE myopathy, i.e. hereditary inclusion body myopathy. Complete Gne knockout is embryonically lethal. Transgenic mice expressing the human GNE cDNA with the D176V mutation, common among Japanese patients, in a mouse background with a disrupted mouse Gne gene recapitulates the adult onset features of human GNE myopathy with hyposialylation in serum and different organs. M712T mouse mutants die within 72 h of birth from severe glomerular disease. Mouse isozyme mutant phenotypes, overview
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metabolism
rate-limiting in the sialic acid biosynthetic pathway
metabolism
sialic acid biosynthesis pathway
metabolism
GNE is the key enzyme of sialic acid biosynthesis
metabolism
the bifunctional enzyme UDP-GlcNAc 2-epimerase/ManNAc kinase, GNE, catalyzes the first two committed steps in sialic acid synthesis
metabolism
UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE) catalyzes the first two committed steps in sialic acid synthesis
metabolism
-
UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase is the key enzyme in the sialic acid biosynthetic pathway
metabolism
the enzyme catalyzes the second step of the sialic acid catabolic pathway
metabolism
-
the bifunctional enzyme UDP-GlcNAc 2-epimerase/ManNAc kinase, GNE, catalyzes the first two committed steps in sialic acid synthesis
-
metabolism
-
the enzyme catalyzes the second step of the sialic acid catabolic pathway
-
physiological function
GNE exerts transcriptional control on genes related to endoplasmic reticulum stress. Association of low GNE activity and anoikis susceptibility
physiological function
-
the bifunctional UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase transforms UDP-N-acetylglucosamine to N-acetylmannosamine followed by its phosphorylation to ManNAc 6-phosphate and has a direct impact on the sialylation of cell surface components
physiological function
the mGne2 encoding transcript is differentially expressed and may act as a tissue-specific regulator of sialylation. mGne2 expression appears significantly increased the first 2 days of life, possibly reflecting the high sialic acid demand during this period
physiological function
-
the mGne2 encoding transcript is differentially expressed and may act as a tissue-specific regulator of sialylation. mGne2 expression appears significantly increased the first 2 days of life, possibly reflecting the high sialic acid demand during this period
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additional information
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active site structure of the N-acetylmannosamine kinase domain, ligand binding and reaction mechanism, catalytic role of Asp517, overview. The side chain of Asp-413 does not directly bind one of the oxygens of the beta-phosphate but is necessary for Mg2+ coordination and consequently crucial for ATP binding
additional information
epimerase enzymatic activity of isozymes GNE3 and GNE8 is likely absent, since the deleted fragment contains important substrate binding residues in homologous bacterial epimerases. Isozymes hGNE5-hGNE8 have a 53-residue deletion, which is assigned a role in substrate(UDP-GlcNAc) binding
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A524V
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30% ManNAc kinase activity of the wild type enzyme
A631T
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75% ManNAc kinase activity of the wild type enzyme
C303V
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60% ManNAc kinase activity of the wild type enzyme
C303X
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no ManNAc kinase activity
D378Y
-
45% ManNAc kinase activity of the wild type enzyme
D517A
site-directed mutagenesis, inactive mutant
D517N
site-directed mutagenesis, inactive mutant
E35X
enzyme activity is severely decreased or absent in this mutant
F528C
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35% ManNAc kinase activity of the wild type enzyme
F537I
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60% ManNAc kinase activity of the wild type enzyme
G135E
enzyme activity is severely decreased or absent in this mutant
G576E
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15% ManNAc kinase activity of the wild type enzyme
G576R
the mutation is associated with distal myopathy with rimmed vacuoles
G708S
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5% ManNAc kinase activity of the wild type enzyme
H132Q
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50% ManNAc kinase activity of the wild type enzyme
I200F
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75% ManNAc kinase activity of the wild type enzyme
I472T
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5% ManNAc kinase activity of the wild type enzyme
I587T
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35% ManNAc kinase activity of the wild type enzyme
M743T
the mutation, which is associated with GNE myopathy, has a 10fold lower binding affinity to alpha-actinin 2 than the intact enzyme
N519S
-
20% ManNAc kinase activity of the wild type enzyme
R11W
-
40% ManNAc kinase activity of the wild type enzyme
R177C
-
80% ManNAc kinase activity of the wild type enzyme
V331A
-
115% ManNAc kinase activity of the wild type enzyme
D176V
oral administration of the sialic acid precursor N-acetylmannosamine rescues the muscle phenotype in the transgenic Gne p.D176V mouse and partially rescues the glomerular disease and early lethality in the knockin Gne mutant M712T mouse model
M712T
naturally occuring mutation of isozyme mGne2. Tissues of the knock-in Gne p.M712T mouse model has similar mGne transcript expression levels among genotypes, indicating no effect of the mutation on mRNA expression, but the mutant shows increased activity in presence of N-acetylmannosamine compared to the wild-type enzyme. M712T mouse mutants die within 72 h of birth from severe glomerular disease
D176V
-
oral administration of the sialic acid precursor N-acetylmannosamine rescues the muscle phenotype in the transgenic Gne p.D176V mouse and partially rescues the glomerular disease and early lethality in the knockin Gne mutant M712T mouse model
-
M712T
-
naturally occuring mutation of isozyme mGne2. Tissues of the knock-in Gne p.M712T mouse model has similar mGne transcript expression levels among genotypes, indicating no effect of the mutation on mRNA expression, but the mutant shows increased activity in presence of N-acetylmannosamine compared to the wild-type enzyme. M712T mouse mutants die within 72 h of birth from severe glomerular disease
-
D413K
-
loss of kinase activity
D413L
-
loss of kinase activity
D413N
-
loss of kinase activity
DELTA1-234
-
monomer molecular mass of 58000 Da, complete loss of epimerase activity, 90% loss of kinase activity
DELTA1-359
-
monomer molecular mass of 45000 Da, complete loss of epimerase activity, almost complete loss of kinase activity
DELTA1-39
-
monomer molecular mass of 79000 Da, complete loss of epimerase activity, 75% loss of kinase activity
DELTA383-722
-
monomer molecular mass of 49000 Da, almost complete loss of epimerase activity, complete loss of kinase activity
DELTA490-722
-
monomer molecular mass of 61000 Da, more than 80% loss of epimerase activity, complete loss of kinase activity
DELTA597-722
-
monomer molecular mass of 72000 Da, almost complete loss of epimerase activity, and kinase activity
DELTA697-722
-
monomer molecular mass of 83000 Da, 25% loss of epimerase activity, 60% loss of kinase activity
DELTA717-722
-
monomer molecular mass of 85000 Da, less than 10% loss of epimerase activity, 20% loss of kinase activity
H110A
-
loss of epimerase activity
H132A
-
loss of epimerase activity
H155A
-
loss of epimerase activity
H157A
-
loss of epimerase activity
H45A
-
loss of epimerase activity
R420M
-
loss of kinase activity
Y160A
the mutant has a higher enzyme specificity (kcat/Km) with GlcNAc than for N-acetylmannosamine
Y160F
the mutant has a higher enzyme specificity (kcat/Km) with GlcNAc than for N-acetylmannosamine
Y160A
-
the mutant has a higher enzyme specificity (kcat/Km) with GlcNAc than for N-acetylmannosamine
-
Y160F
-
the mutant has a higher enzyme specificity (kcat/Km) with GlcNAc than for N-acetylmannosamine
-
A630T
-
40% ManNAc kinase activity of the wild type enzyme
A630T
homozygous mutant of the N-acetylmannose kinase domain, involved in GNE myopathy
A631V
-
15% ManNAc kinase activity of the wild type enzyme
A631V
-
65% ManNAc kinase activity of the wild type enzyme
C13S
-
105% ManNAc kinase activity of the wild type enzyme
C13S
the mutation is associated with distal myopathy with rimmed vacuoles
D176V
-
85% ManNAc kinase activity of the wild type enzyme
D176V
the mutation leads to impaired N-acetylmannosamine kinase activity (40.58% of wild type activity)
M712T
naturally occurring mutation, 30% loss of kinase activity
M712T
-
70% ManNAc kinase activity of the wild type enzyme
M712T
homozygous mutant of the N-acetylmannose kinase domain, involved in GNE myopathy
V572L
-
10% ManNAc kinase activity of the wild type enzyme
V572L
homozygous mutant of the N-acetylmannose kinase domain, involved in GNE myopathy
V572L
the mutation leads to impaired N-acetylmannosamine kinase activity (15.9% of wild type activity)
additional information
-
different mutations found in patients with distal myopathy with rimmed vacuoles, D378Y, V331A, D177C, D176V, H132Q and C13S in the epimerase domain are mostly without effect on the kinase activity, V572L, A524V, I472T, A630T, A631V, and G708S in the kinase domain some of which causes a dramatic decrease of kinase activity, some of the mutations affects both activities
additional information
-
naturally occurring mutations in patients with hereditary inclusion body myopathy, mutations G135V, V216A, R246W, A631V, and M217T identified, mutations severely affect both activities of the bifunctional enzyme
additional information
homozygote and heterozygte mutants of the epimerase and the kinase domains of the enzyme, respectively, overview
additional information
-
stable knock-down of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase in HEK-293 cells by RNAi dramatically increases incorporation of N-acetylmannosamine analogues into glycoproteins of HEK-293 cells. HEK293 cells transfected with sh68- and sh70-shRNA almost completely loose GNE mRNA expression, while other shRNAs are less effective. Peanut agglutinin, recognizing asialo structures, reveals a 3-4fold higher binding affinity to GNE knock-down cells compared to controls
additional information
the enzyme is silenced or overexpressed in human pancreatic carcinoma cells, gene expression profiling, enzymatic activity, transcriptions levels, and cell cycle analysis, overview
additional information
-
the enzyme is silenced or overexpressed in human pancreatic carcinoma cells, gene expression profiling, enzymatic activity, transcriptions levels, and cell cycle analysis, overview
additional information
-
heterozygous mice deficient for bifunctional UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase display a organ-specific reduction of membrane-bound sialic acids of about 25%. Transferrin expression is unchanged in heterozygous mice, but the isoelectric point of transferrin is shifted towards basic pH value. The expression of polysialic acids on polysialylated neural cell adhesion molecule is reduced
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