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dihydropyrimidine-2,4(1H,3H)-dione-alpha-D-ribofuranosyl-5'-diphospho-2-acetamido-2-deoxy-alpha-D-mannopyranoside
?
N-Acetyl-D-glucosamine
?
-
-
-
-
?
N-Acetyl-D-glucosamine 1-phosphate
?
-
-
-
-
?
UDP-GlcNAc + H2O
ManNAc + UDP
-
biosynthesis of sialic acids
-
-
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
UDP-N-acetyl-alpha-D-mannosamine
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-D-glucosamine
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
UDP-N-acetyl-D-glucosamine + H2O
UDP + N-acetylmannosamine
UDP-N-acetylgalactosamine
?
-
-
-
-
?
uridine 5'-diphospho-2-hydroxyacetamido-2-deoxy-alpha-D-mannopyranoside
?
uridine 5'-diphospho-2-propionamido-2-deoxy-alpha-D-mannopyranoside
?
Neisseria meningitidis serogroup A / serotype 4A
-
-
-
?
uridine 5'-diphospho-N-trifluoroaceto-2-deoxy-alpha-D-mannopyranoside
?
Neisseria meningitidis serogroup A / serotype 4A
-
-
-
?
additional information
?
-
dihydropyrimidine-2,4(1H,3H)-dione-alpha-D-ribofuranosyl-5'-diphospho-2-acetamido-2-deoxy-alpha-D-mannopyranoside
?
Neisseria meningitidis serogroup A / serotype 4A
-
-
-
?
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
-
-
-
?
UDP-GlcNAc
ManNAc + UDP
biosynthetic pathway of sialic acid
-
-
?
UDP-GlcNAc
ManNAc + UDP
-
sialic acid biosynthetic pathway
-
-
?
UDP-GlcNAc
ManNAc + UDP
-
biosynthesis of sialic acid
-
-
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
Q81K32
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
Q81X16
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
Q81K32
allosteric regulatory mechanism, which involves direct interaction between one substrate molecule in the active site and another in the allosteric site
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
UDP-GlcNAc binding structure, overview
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
UDP-GlcNAc binding structure, overview
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
UDP-GlcNAc binding structure, overview
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
Neisseria meningitidis serogroup A / serotype 4A
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
Neisseria meningitidis serogroup A / serotype 4A Z2491
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
Neisseria meningitidis serogroup A /serotype 4A
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
Neisseria meningitidis serogroup A /serotype 4A
interconversion
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
Neisseria meningitidis serogroup A /serotype 4A Z2491
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
Neisseria meningitidis serogroup A /serotype 4A Z2491
interconversion
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
allosteric regulatory mechanism, which involves direct interaction between one substrate molecule in the active site and another in the allosteric site
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
interconversion
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
interconversion
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
-
interconversion
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
-
interconversion
-
-
r
UDP-N-acetyl-alpha-D-mannosamine
UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-mannosamine
UDP-N-acetyl-alpha-D-glucosamine
-
-
-
-
r
UDP-N-acetyl-alpha-D-mannosamine
UDP-N-acetyl-alpha-D-glucosamine
Neisseria meningitidis serogroup A / serotype 4A
-
-
-
r
UDP-N-acetyl-alpha-D-mannosamine
UDP-N-acetyl-alpha-D-glucosamine
Neisseria meningitidis serogroup A / serotype 4A Z2491
-
-
-
r
UDP-N-acetyl-alpha-D-mannosamine
UDP-N-acetyl-alpha-D-glucosamine
Neisseria meningitidis serogroup A /serotype 4A
interconversion
-
-
r
UDP-N-acetyl-alpha-D-mannosamine
UDP-N-acetyl-alpha-D-glucosamine
Neisseria meningitidis serogroup A /serotype 4A Z2491
interconversion
-
-
r
UDP-N-acetyl-alpha-D-mannosamine
UDP-N-acetyl-alpha-D-glucosamine
interconversion
-
-
r
UDP-N-acetyl-alpha-D-mannosamine
UDP-N-acetyl-alpha-D-glucosamine
interconversion
-
-
r
UDP-N-acetyl-alpha-D-mannosamine
UDP-N-acetyl-alpha-D-glucosamine
-
interconversion
-
-
r
UDP-N-acetyl-alpha-D-mannosamine
UDP-N-acetyl-alpha-D-glucosamine
-
interconversion
-
-
r
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
-
-
?
UDP-N-acetyl-D-glucosamine
?
-
enzyme of the N-acetylneuraminic acid metabolic pathway
-
-
?
UDP-N-acetyl-D-glucosamine
?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine
?
-
enzyme of biosynthesis of N-acetylneuraminic acid
-
-
?
UDP-N-acetyl-D-glucosamine
?
-
initial enzyme responsible for the biosynthesis of CMP-N-acetylneuraminic acid
-
-
?
UDP-N-acetyl-D-glucosamine
?
-
possible role in the biogenesis of N-acetylmannosamine-containing macromolecules
-
-
?
UDP-N-acetyl-D-glucosamine
?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
non-hydrolizing
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
the reverse reaction with UDP-N-acetylmannosamine requires the presence of UDP-N-acetylglucosamine
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
-
-
-
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
r
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
the reverse reaction with UDP-N-acetylmannosamine requires the presence of UDP-N-acetylglucosamine
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
the reverse reaction with UDP-N-acetylmannosamine requires the presence of UDP-N-acetylglucosamine
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
the reverse reaction with UDP-N-acetylmannosamine requires the presence of UDP-N-acetylglucosamine
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
reduction of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase activity and sialylation in distal myopathy with rimmed vacuoles
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
-
-
r
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
first step of sialic acid biosynthesis
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
mechanism involves an anti elimination of UDP to form 2-acetamidoglucal as an intermediate, followed by syn-addition of water
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
first step of sialic acid biosynthesis
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
mechanism involves an anti elimination of UDP to form 2-acetamidoglucal as an intermediate, followed by syn-addition of water
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
-
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
reversibility is not detected
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
reversibility is not detected
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
key enzyme of sialic acid biosynthesis
-
-
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
characterization of ligand binding to the bifunctional enzyme
-
-
?
UDP-N-acetyl-D-glucosamine + H2O
UDP + N-acetylmannosamine
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + H2O
UDP + N-acetylmannosamine
-
-
-
?
UDP-N-acetyl-D-glucosamine + H2O
UDP + N-acetylmannosamine
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
-
-
?
UDP-N-acetyl-D-glucosamine + H2O
UDP + N-acetylmannosamine
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + H2O
UDP + N-acetylmannosamine
-
-
-
-
?
uridine 5'-diphospho-2-hydroxyacetamido-2-deoxy-alpha-D-mannopyranoside
?
Neisseria meningitidis serogroup A / serotype 4A
-
-
-
?
uridine 5'-diphospho-2-hydroxyacetamido-2-deoxy-alpha-D-mannopyranoside
?
Neisseria meningitidis serogroup A / serotype 4A Z2491
-
-
-
?
additional information
?
-
-
3'-deoxy-UDP-N-acetylglucosamine is not a substrate
-
-
?
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
-
?
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
-
?
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
-
-
?
additional information
?
-
-
the bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase is a rate-limiting enzyme of sialic acid biosynthesis
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
biosynthesis of sialic acids
-
-
?
additional information
?
-
-
biosynthesis of sialic acids
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
GNE is a bifunctional enzyme with UDP-GlcNAc 2-epimerase and ManNAc kinase activities
-
-
?
additional information
?
-
-
GNE is a bifunctional enzyme with UDP-GlcNAc 2-epimerase and ManNAc kinase activities
-
-
?
additional information
?
-
-
GNE is a bifunctional enzyme with UDP-GlcNAc 2-epimerase and ManNAc kinase activities
-
-
?
additional information
?
-
GNE is a bifunctional enzyme with UDP-GlcNAc 2-epimerase and ManNAc kinase activities
-
-
?
additional information
?
-
-
GNE is a bifunctional enzyme with UDP-GlcNAc 2-epimerase and ManNAc kinase activities
-
-
?
additional information
?
-
biosynthesis of sialic acids
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
GNE is a bifunctional enzyme with UDP-GlcNAc 2-epimerase and ManNAc kinase activities
-
-
?
additional information
?
-
-
GNE is a bifunctional enzyme with UDP-GlcNAc 2-epimerase and ManNAc kinase activities
-
-
?
additional information
?
-
Neisseria meningitidis serogroup A / serotype 4A
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
-
-
?
additional information
?
-
Neisseria meningitidis serogroup A / serotype 4A Z2491
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
-
-
?
additional information
?
-
Neisseria meningitidis serogroup A /serotype 4A
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
-
-
?
additional information
?
-
Neisseria meningitidis serogroup A /serotype 4A Z2491
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
-
-
?
additional information
?
-
-
bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
-
?
additional information
?
-
-
enzyme catalyzes the first step in synthesis of sialic acids
-
?
additional information
?
-
-
reaction mechanism involving an anti-elimination of UDP to give 2-acetamidoglucal, followed by a syn-addition of water
-
?
additional information
?
-
-
key enzyme of N-acetylneuraminic acid biosynthesis
-
?
additional information
?
-
-
the bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/ManNAc kinase catalyzes the first two steps in the biosynthesis of the sialic acids
-
?
additional information
?
-
-
the enzyme catalyzes the first step of sialic acid biosynthesis
-
?
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
-
-
?
additional information
?
-
-
GNE is a bifunctional enzyme with UDP-GlcNAc 2-epimerase and ManNAc kinase activities
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UDP-GlcNAc + H2O
ManNAc + UDP
-
biosynthesis of sialic acids
-
-
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
UDP-N-acetyl-D-glucosamine
?
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
UDP-N-acetyl-D-glucosamine + H2O
UDP + N-acetylmannosamine
additional information
?
-
UDP-GlcNAc
ManNAc + UDP
biosynthetic pathway of sialic acid
-
-
?
UDP-GlcNAc
ManNAc + UDP
-
sialic acid biosynthetic pathway
-
-
?
UDP-GlcNAc
ManNAc + UDP
-
biosynthesis of sialic acid
-
-
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
Q81K32, Q81X16
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
Q81K32
allosteric regulatory mechanism, which involves direct interaction between one substrate molecule in the active site and another in the allosteric site
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UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
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UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
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UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
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UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
Neisseria meningitidis serogroup A / serotype 4A
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UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
Neisseria meningitidis serogroup A / serotype 4A Z2491
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UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
Neisseria meningitidis serogroup A /serotype 4A
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UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
Neisseria meningitidis serogroup A /serotype 4A Z2491
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UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
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UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
allosteric regulatory mechanism, which involves direct interaction between one substrate molecule in the active site and another in the allosteric site
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r
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
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UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
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UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
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UDP-N-acetyl-D-glucosamine
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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
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UDP-N-acetyl-D-glucosamine
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enzyme of the N-acetylneuraminic acid metabolic pathway
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UDP-N-acetyl-D-glucosamine
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UDP-N-acetyl-D-glucosamine
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enzyme of biosynthesis of N-acetylneuraminic acid
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UDP-N-acetyl-D-glucosamine
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initial enzyme responsible for the biosynthesis of CMP-N-acetylneuraminic acid
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UDP-N-acetyl-D-glucosamine
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possible role in the biogenesis of N-acetylmannosamine-containing macromolecules
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UDP-N-acetyl-D-glucosamine
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UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
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reduction of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase activity and sialylation in distal myopathy with rimmed vacuoles
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UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
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first step of sialic acid biosynthesis
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UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
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first step of sialic acid biosynthesis
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UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
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key enzyme of sialic acid biosynthesis
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UDP-N-acetyl-D-glucosamine + H2O
UDP + N-acetylmannosamine
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UDP-N-acetyl-D-glucosamine + H2O
UDP + N-acetylmannosamine
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UDP-N-acetyl-D-glucosamine + H2O
UDP + N-acetylmannosamine
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UDP-N-acetyl-D-glucosamine + H2O
UDP + N-acetylmannosamine
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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the bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase is a rate-limiting enzyme of sialic acid biosynthesis
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additional information
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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
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additional information
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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
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additional information
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biosynthesis of sialic acids
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additional information
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biosynthesis of sialic acids
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additional information
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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
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additional information
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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
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additional information
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biosynthesis of sialic acids
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additional information
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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
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additional information
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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
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additional information
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key enzyme of N-acetylneuraminic acid biosynthesis
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additional information
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the bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/ManNAc kinase catalyzes the first two steps in the biosynthesis of the sialic acids
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additional information
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the enzyme catalyzes the first step of sialic acid biosynthesis
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additional information
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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
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(2S)-2-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanamide
(2S)-2-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
(2S)-2-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]butanoic acid
(2S)-2-[(4E)-4-[[5-(3,4-dichlorophenyl)thiophen-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
(2S)-2-[(4E)-4-[[5-(3,5-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
(2S)-2-[(4E)-4-[[5-(3-chloro-4-methoxyphenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
(2S)-2-[(4E)-4-[[5-(3-chlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
(2S)-2-[(4E)-4-[[5-(4-bromo-3-chlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
(2S)-2-[(4E)-4-[[5-(4-bromo-3-chlorophenyl)thiophen-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
(2S)-2-[(4E)-4-[[5-(4-bromophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
(2S)-2-[(4E)-4-[[5-(4-bromophenyl)thiophen-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
(2S)-2-[(4E)-4-[[5-(4-chlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
(2S)-2-[(4E)-4-[[5-(4-chlorophenyl)thiophen-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
(2S)-2-[(4E)-4-[[5-(4-fluorophenyl)thiophen-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
(2S)-2-[(4E)-4-[[5-(4-iodophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
(2S)-2-[(4E)-4-[[5-(4-methoxyphenyl)thiophen-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
(2S)-2-[(4E)-5-oxo-2-thioxo-4-([5-[4-(trifluoromethoxy)phenyl]furan-2-yl]methylidene)imidazolidin-1-yl]-3-phenylpropanoic acid
(2S)-2-[(4E)-5-oxo-4-[(5-phenylfuran-2-yl)methylidene]-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
2',3'-dialdehydro-ADP
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efficient inhibition is most likely due to the structural similarity to o-UDP and not to an allosteric effect via the ATP binding site
2',3'-dialdehydro-UDP
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binds to the active site of the enzyme
2',3'-dialdehydro-UDP-alpha-D-N-acetylglucosamine
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0.05 mM, 70% inhibition after 30 min. 0.25 mM, 90% inhibition. Covalently bound to amino acids in the active site causing an irreversible inhibition. Effective inhibitor may serve as a basis for the chemical synthesis of further inhibitors
3-acetamido-2,6-anhydro-3-deoxy-D-arabino-hept-2-enopyranosonate
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CMP-N-acetylneuraminic acid
CMP-sialic acid
GNE/MNK is feedback inhibited by binding of the downstream product, CMP-sialic acid, in its allosteric site. The allosteric regulation by CMP-sialic acid involves residues D255, E260, R263, R266, K268, and N275
ethyl (2S)-2-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoate
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ethyl (2S)-2-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoates
Q81K32
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N-[1-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-2-phenylethyl]-1,1,1-trifluoromethanesulfonamide
N-[1-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-2-phenylethyl]methanesulfonamide
N-[1-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]propyl]methanesulfonamide
uridine 5'-(3-acetamido-3-deoxy-2-O-methyl-alpha-D-gluco-hept-2-ulopyranos-1-yl diphosphate)
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uridine 5'-(3-acetamido-3-deoxy-2-O-methyl-alpha-D-manno-hept-2-ulopyranos-1-yl diphosphate)
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weak
uridine 5'-[(Z)-2,6-anhydro-1-deoxy-D-galactohept-1-enitol-1-yl phosphono] phosphate
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weak
uridine 5'-[(Z)-2,6-anhydro-1-deoxy-D-glucohept-1-enitol-1-yl phosphono] phosphate
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uridine 5'-[(Z)-2,6-anhydro-1-deoxy-D-mannohept-1-enitol-1-yl phosphono] phosphate
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uridine 5'-[(Z)-3-acetamido-2,6-anhydro-1,3-dideoxy-D-arabino-hept-1-enitol-1-yl phosphono] phosphate
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uridine 5'-[(Z)-3-acetamido-2,6-anhydro-1,3-dideoxy-D-gluco-hept-1-enitol-1-yl phosphono] phosphate
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[1-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-2-phenylethyl]cyanamide
(2S)-2-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanamide
Q81K32
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(2S)-2-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanamide
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(2S)-2-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
Q81K32
i.e. Epimerox, 2-epimerase inhibition through a target-specific mechanism, in vivo efficacy against Staphylococcus aureus and Bacillus anthracis
(2S)-2-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
i.e. Epimerox, 2-epimerase inhibition through a target-specific mechanism, in vivo efficacy against Staphylococcus aureus and Bacillus anthracis
(2S)-2-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]butanoic acid
Q81K32
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(2S)-2-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]butanoic acid
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(2S)-2-[(4E)-4-[[5-(3,4-dichlorophenyl)thiophen-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
Q81K32
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(2S)-2-[(4E)-4-[[5-(3,4-dichlorophenyl)thiophen-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
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(2S)-2-[(4E)-4-[[5-(3,5-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
Q81K32
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(2S)-2-[(4E)-4-[[5-(3,5-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
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(2S)-2-[(4E)-4-[[5-(3-chloro-4-methoxyphenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
Q81K32
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(2S)-2-[(4E)-4-[[5-(3-chloro-4-methoxyphenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
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(2S)-2-[(4E)-4-[[5-(3-chlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
Q81K32
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(2S)-2-[(4E)-4-[[5-(3-chlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
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(2S)-2-[(4E)-4-[[5-(4-bromo-3-chlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
Q81K32
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(2S)-2-[(4E)-4-[[5-(4-bromo-3-chlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
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(2S)-2-[(4E)-4-[[5-(4-bromo-3-chlorophenyl)thiophen-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
Q81K32
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(2S)-2-[(4E)-4-[[5-(4-bromo-3-chlorophenyl)thiophen-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
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(2S)-2-[(4E)-4-[[5-(4-bromophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
Q81K32
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(2S)-2-[(4E)-4-[[5-(4-bromophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
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(2S)-2-[(4E)-4-[[5-(4-bromophenyl)thiophen-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
Q81K32
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(2S)-2-[(4E)-4-[[5-(4-bromophenyl)thiophen-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
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(2S)-2-[(4E)-4-[[5-(4-chlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
Q81K32
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(2S)-2-[(4E)-4-[[5-(4-chlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
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(2S)-2-[(4E)-4-[[5-(4-chlorophenyl)thiophen-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
Q81K32
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(2S)-2-[(4E)-4-[[5-(4-chlorophenyl)thiophen-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
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(2S)-2-[(4E)-4-[[5-(4-fluorophenyl)thiophen-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
Q81K32
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(2S)-2-[(4E)-4-[[5-(4-fluorophenyl)thiophen-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
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(2S)-2-[(4E)-4-[[5-(4-iodophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
Q81K32
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(2S)-2-[(4E)-4-[[5-(4-iodophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
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(2S)-2-[(4E)-4-[[5-(4-methoxyphenyl)thiophen-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
Q81K32
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(2S)-2-[(4E)-4-[[5-(4-methoxyphenyl)thiophen-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
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(2S)-2-[(4E)-5-oxo-2-thioxo-4-([5-[4-(trifluoromethoxy)phenyl]furan-2-yl]methylidene)imidazolidin-1-yl]-3-phenylpropanoic acid
Q81K32
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(2S)-2-[(4E)-5-oxo-2-thioxo-4-([5-[4-(trifluoromethoxy)phenyl]furan-2-yl]methylidene)imidazolidin-1-yl]-3-phenylpropanoic acid
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(2S)-2-[(4E)-5-oxo-4-[(5-phenylfuran-2-yl)methylidene]-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
Q81K32
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(2S)-2-[(4E)-5-oxo-4-[(5-phenylfuran-2-yl)methylidene]-2-thioxoimidazolidin-1-yl]-3-phenylpropanoic acid
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2-acetamidoglucal
Neisseria meningitidis serogroup A / serotype 4A
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2-acetamidoglucal
Neisseria meningitidis serogroup A /serotype 4A
recombinant enzyme
Ca2+
Neisseria meningitidis serogroup A / serotype 4A
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Ca2+
Neisseria meningitidis serogroup A /serotype 4A
slight inhibition at 10 mM
CMP-N-acetylneuraminic acid
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CMP-N-acetylneuraminic acid
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50% inhibition by 0.025 mM
CMP-N-acetylneuraminic acid
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CMP-N-acetylneuraminic acid
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feedback inhibitor
CMP-Neu5Ac
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feedback inhibition
CMP-Neu5Ac
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feedback inhibition
CMP-Neu5Ac
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allosterical feed-back-inhibition
CMP-Neu5Ac
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feedback inhibition
Co2+
Neisseria meningitidis serogroup A /serotype 4A
strong inhibition at 10 mM
Cu2+
Neisseria meningitidis serogroup A / serotype 4A
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Cu2+
Neisseria meningitidis serogroup A /serotype 4A
slight inhibition at 10 mM
Mg2+
Neisseria meningitidis serogroup A / serotype 4A
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Mg2+
Neisseria meningitidis serogroup A /serotype 4A
slight inhibition at 10 mM
Mn2+
Neisseria meningitidis serogroup A / serotype 4A
leads to enzyme precipitation at 10 mM
Mn2+
Neisseria meningitidis serogroup A /serotype 4A
complete inhibition at 10 mM, the epimerase and the activity cannot be rescued by subsequent addition of EDTA
N-[1-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-2-phenylethyl]-1,1,1-trifluoromethanesulfonamide
Q81K32
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N-[1-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-2-phenylethyl]-1,1,1-trifluoromethanesulfonamide
-
N-[1-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-2-phenylethyl]methanesulfonamide
Q81K32
-
N-[1-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-2-phenylethyl]methanesulfonamide
-
N-[1-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]propyl]methanesulfonamide
Q81K32
-
N-[1-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]propyl]methanesulfonamide
-
Ni2+
Neisseria meningitidis serogroup A / serotype 4A
-
Ni2+
Neisseria meningitidis serogroup A /serotype 4A
slight inhibition at 10 mM
PCMB
-
-
tunicamycin
the natural product antibiotic physically binds Cap5P and inhibits 2-epimerase activity, NMR study, reversible inhibition; the natural product antibiotic physically binds MnaA and inhibits 2-epimerase activity, NMR study, reversible inhibition
tunicamycin
-
the natural product antibiotic physically binds MnaA and inhibits 2-epimerase activity, NMR study, reversible inhibition
UDP
-
-
UDP
binding structure, overview
UDP
binding structure, overview
UDP
Neisseria meningitidis serogroup A / serotype 4A
-
UDP
Neisseria meningitidis serogroup A /serotype 4A
recombinant enzyme
UDP
-
competitive inhibition
Zn2+
Neisseria meningitidis serogroup A / serotype 4A
leads to enzyme precipitation at 10 mM
Zn2+
Neisseria meningitidis serogroup A /serotype 4A
complete inhibition at 10 mM, the epimerase and the activity cannot be rescued by subsequent addition of EDTA
[1-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-2-phenylethyl]cyanamide
Q81K32
-
[1-[(4E)-4-[[5-(3,4-dichlorophenyl)furan-2-yl]methylidene]-5-oxo-2-thioxoimidazolidin-1-yl]-2-phenylethyl]cyanamide
-
additional information
Q81K32
synthesis and evaluation of specific inhibitors, overview
-
additional information
-
UDP-glycal derivatives as transition state analogues of GNE substrates are synthesized, especially UDP-exo-glycal derivatives, C-glycosidic derivatives of 2-acetamidoglucal, and ketosides as bisubstrate analogues and bis-product analogues, respectively. Derivatives of 1-deoxyiminosugars with and without substitution of the iminogroup in the ring are promising GNE inhibitors, designed as transition-state analogues of the known enzymatic mechanism of UDP-GlcNAc 2-epimerase
-
additional information
-
UDP-glycal derivatives as transition state analogues of GNE substrates are synthesized, especially UDP-exo-glycal derivatives, C-glycosidic derivatives of 2-acetamidoglucal, and ketosides as bisubstrate analogues and bis-product analogues, respectively. Derivatives of 1-deoxyiminosugars with and without substitution of the iminogroup in the ring are promising GNE inhibitors, designed as transition-state analogues of the known enzymatic mechanism of UDP-GlcNAc 2-epimerase
-
additional information
Neisseria meningitidis serogroup A / serotype 4A
both 2-acetamidoglucal and UDP show competitive inhibitory effects for the UDP-ManNAc 2-epimerization of NmSacA-His6. No inhibition by EDTA, and 1 mM DTT
-
additional information
-
UDP-glycal derivatives as transition state analogues of GNE substrates are synthesized, especially UDP-exo-glycal derivatives, C-glycosidic derivatives of 2-acetamidoglucal, and ketosides as bissubstrate analogues and bis-product analogues, respectively. Derivatives of 1-deoxyiminosugars with and without substitution of the iminogroup in the ring are promising GNE inhibitors, designed as transition-state analogues of the known enzymatic mechanism of UDP-GlcNAc 2-epimerase
-
additional information
synthesis and evaluation of specific inhibitors, overview
-
additional information
-
synthesis and evaluation of specific inhibitors, overview
-
additional information
WTA 2-epimerases are dual beta-lactam potentiation and antibiofilm drug targets; WTA 2-epimerases are dual beta-lactam potentiation and antibiofilm drug targets
-
additional information
WTA 2-epimerases are dual beta-lactam potentiation and antibiofilm drug targets; WTA 2-epimerases are dual beta-lactam potentiation and antibiofilm drug targets
-
additional information
-
WTA 2-epimerases are dual beta-lactam potentiation and antibiofilm drug targets; WTA 2-epimerases are dual beta-lactam potentiation and antibiofilm drug targets
-
additional information
-
WTA 2-epimerases are dual beta-lactam potentiation and antibiofilm drug targets
-
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evolution
Q81K32
the bacterial UDP-GlcNAc-binding site is conserved and probably unique to the nonhydrolyzing bacterial 2-epimerases. Conservation of the allosteric site residues in the nonhydrolyzing bacterial 2-epimerases indicates that the allosteric regulatory mechanism, which involves direct interaction between one substrate molecule in the active site and another in the allosteric site, is used exclusively by this class of bacterial enzymes
evolution
the bacterial UDP-GlcNAc-binding site is conserved and probably unique to the nonhydrolyzing bacterial 2-epimerases. Conservation of the allosteric site residues in the nonhydrolyzing bacterial 2-epimerases indicates that the allosteric regulatory mechanism, which involves direct interaction between one substrate molecule in the active site and another in the allosteric site, is used exclusively by this class of bacterial enzymes
evolution
Q81K32, Q81X16
Bacillus anthracis gneY and gneZ encode nearly identical UDP-GlcNAc 2-epimerase enzymes that catalyze the reversible conversion of UDPGlcNAc and UDP-ManNAc
malfunction
-
enzyme deficiency causes the disease sialuria in humans. Hereditary inclusion body myopathy, h-IBM, is also a disease caused by different mutations in the GNE gene, it is an autosomal recessive neuromuscular disorder characterized by adult onset, slowly progressive skeletal muscle weakness, and typical histological features as rimmed vacuoles and filamentous inclusions. Sialuria is caused by the loss of feedback control of UDP-GlcNAc 2-epimerase activity due to the mutation of only one of the two arginine residues 263 and 266. Sialuria leads to massive production of free Neu5Ac, which accumulates in the cytoplasm and results in mental retardation and hepatomegaly
malfunction
-
GNE deficiency can lead to hereditary inclusion body myopathy, HIBM, phenotypes, overview
malfunction
GNE mutations can result in two human disorders, hereditary inclusion body myopathy, HIBM, and sialuria
malfunction
-
inactivation of GNE causes early embryonic lethality
malfunction
-
mutations in the GNE gene are associated with autosomal recessive hereditary inclusion body myopathy, i.e. HIBM or IBM2, a progressive adult onset muscle wasting disorder characterized by sparing of the quadriceps. IBM2 is also known as distal myopathy with rimmed vacuoles or nonaka myopathy
malfunction
-
stable knock-down of GNE dramatically increases incorporation of N-acetylmannosamine analogues into glycoproteins of HEK-293 cells
malfunction
mutation of this enzyme causes changes in cell morphology and the thermoresistance of the cell wall
malfunction
mutation of this enzyme causes changes in cell morphology and the thermoresistance of the cell wall
malfunction
deletions of early wall teichoic acid (WTA) biosynthetic enzymes are nonlethal, but cause diverse attenuated virulence phenotypes, deletions of later steps in WTA biosynthesis are not generally tolerated and the enzymes are normally essential for growth, an essential gene paradox. The beta-lactam antibiotic imipenem exhibits restored bactericidal activity against mnaA mutants in vitro and concomitant efficacy against 2-epimerase defective strains in a mouse thigh model of MRSA infection. Complementing DELTAcap5P mnaASa P12L and DELTAcap5P mnaASa Y194* with either cap5P or mnaASa reintroduced on an inducible plasmid restores WTA polymer levels, resistance to each of the beta-lactams tested, and wild-type sensitivity to L638
malfunction
-
deletions of early wall teichoic acid (WTA) biosynthetic enzymes are nonlethal, but cause diverse attenuated virulence phenotypes, deletions of later steps in WTA biosynthesis are not generally tolerated and the enzymes are normally essential for growth, an essential gene paradox. The beta-lactam antibiotic imipenem exhibits restored bactericidal activity against mnaA mutants in vitro and concomitant efficacy against 2-epimerase defective strains in a mouse thigh model of MRSE infection
malfunction
-
mutation of this enzyme causes changes in cell morphology and the thermoresistance of the cell wall
-
malfunction
-
deletions of early wall teichoic acid (WTA) biosynthetic enzymes are nonlethal, but cause diverse attenuated virulence phenotypes, deletions of later steps in WTA biosynthesis are not generally tolerated and the enzymes are normally essential for growth, an essential gene paradox. The beta-lactam antibiotic imipenem exhibits restored bactericidal activity against mnaA mutants in vitro and concomitant efficacy against 2-epimerase defective strains in a mouse thigh model of MRSA infection. Complementing DELTAcap5P mnaASa P12L and DELTAcap5P mnaASa Y194* with either cap5P or mnaASa reintroduced on an inducible plasmid restores WTA polymer levels, resistance to each of the beta-lactams tested, and wild-type sensitivity to L638
-
malfunction
-
deletions of early wall teichoic acid (WTA) biosynthetic enzymes are nonlethal, but cause diverse attenuated virulence phenotypes, deletions of later steps in WTA biosynthesis are not generally tolerated and the enzymes are normally essential for growth, an essential gene paradox. The beta-lactam antibiotic imipenem exhibits restored bactericidal activity against mnaA mutants in vitro and concomitant efficacy against 2-epimerase defective strains in a mouse thigh model of MRSE infection
-
metabolism
GNE catalyzes the first two committed, rate-limiting steps in the biosynthesis of N-acetylneuraminic acid, i.e. sialic acid
metabolism
-
GNE catalyzes the first two steps of sialic acid biosynthesis in the cytosol
metabolism
-
GNE is the rate-limiting enzyme of N-acetylneuraminate, i.e. sialic acid, biosynthesis
metabolism
-
the enzyme catalyzes the first two steps in the sialic acid biosynthesis, required for sialylation of diverse glycoproteins and glycolipids e.g. in skeletal muscle
metabolism
-
GNE is the key enzyme in the sialic acid biosynthetic pathway
metabolism
the enzyme catalyzes the interconversion of UDP-N-acetyl-alpha-D-glucosamine to UDP-N-acetyl-alpha-D-mannosamine, which is used in the biosynthesis of cell surface polysaccharides in bacteria
metabolism
-
the enzyme catalyzes the interconversion of UDP-N-acetyl-alpha-D-glucosamine to UDP-N-acetyl-alpha-D-mannosamine, which is used in the biosynthesis of cell surface polysaccharides in bacteria
-
physiological function
-
GNE is required for sialic acid biosynthesis, the sialic acid pathway and the respective sialic acid precursors such as ManNAc do regulate the MAP kinase signalling pathway, influencing processes like cell proliferation, overview
physiological function
-
the bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, GNE, is the key enzyme for the biosynthesis of N-acetylneuraminic acid, from which all other sialic acids are formed
physiological function
-
the bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, GNE, is the key enzyme for the biosynthesis of N-acetylneuraminic acid, from which all other sialic acids are formed
physiological function
-
the bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, GNE, is the key enzyme for the biosynthesis of N-acetylneuraminic acid, from which all other sialic acids are formed
physiological function
Q81K32, Q81X16
GneZ, a UDP-GlcNAc 2-epimerase, is required for S-layer assembly and vegetative growth of Bacillus anthracis. Gene gneZ, but not gneY, is required for Bacillus anthracis vegetative growth, rod cell shape, S-layer assembly, and synthesis of pyruvylated secondary cell wall polysaccharide (SCWP). Nevertheless, inducible expression of gneY alleviates all the defects associated with the gneZ mutant. In contrast to vegetative growth, neither germination of Bacillus anthracis spores nor the formation of spores in mother cells require UDP-GlcNAc 2-epimerase activity. UDP-GlcNAc 2-epimerase enzymes have been shown to be required for the attachment of the phage lysin PlyG with the bacterial envelope and for bacterial growth. UDG-GlcNAc 2-epimerase activity, i.e., the expression of either gneY or gneZ, is not required for B. anthracis spore formation
physiological function
Neisseria meningitidis serogroup A / serotype 4A
SacA is proposed to be involved in the first step in serogroup A capsular polysaccharides (CPS) biosynthetic pathway and is critical for serogroup A CPS biosynthesis. It catalyzes the interconversion between UDP-GlcNAc and UDP-ManNAc. This epimerization process is independent of nicotinamide adenine dinucleotide oxidized form (NAD+) and is critical for synthesizing bacterial ManNAc-containing CPSs
physiological function
UDP-GlcNAc 2-epimerase catalyzes the interconversion of UDP-GlcNAc to UDP-ManNAc, which is used in the biosynthesis of cell surface polysaccharides in bacteria
physiological function
UDP-GlcNAc 2-epimerase catalyzes the interconversion of UDP-GlcNAc to UDP-ManNAc, which is used in the biosynthesis of cell surface polysaccharides in bacteria
physiological function
2-epimerase MnaA interconverts UDP-GlcNAc and UDP-ManNAc to modulate substrate levels of TarO and TarA wall teichoic acid (WTA) biosynthesis enzymes. Besides MnaA, Staphylococcus aureus maintains a second 2-epimerase involved in serotype 5 capsular polysaccharide (CP5) synthesis, Cap5P. MnaA and Cap5P provide compensatory WTA functional roles in Staphylococcus aureus. MnaA and other enzymes of WTA biosynthesis are required for biofilm formation in MRSA. Overlapping functional activity of MnaA and Cap5P in Staphylococci
physiological function
-
2-epimerase MnaA interconverts UDP-GlcNAc and UDP-ManNAc to modulate substrate levels of TarO and TarA wall teichoic acid (WTA) biosynthesis enzymes. MnaA serves as the sole 2-epimerase required for WTA biosynthesis in Staphylococcus epidermidis. MnaA and other enzymes of WTA biosynthesis are required for biofilm formation in MRSE
physiological function
Neisseria meningitidis serogroup A /serotype 4A
Neisseria meningitidis serogroup A non-hydrolyzing UDP-GlcNAc 2-epimerase (NmSacA) catalyzes the interconversion between UDP-GlcNAc and uridine 5?-diphosphate-N-acetylmannosamine (UDP-ManNAc). It is a key enzyme involved in the biosynthesis of the capsular polysaccharide [-6ManNAc?1-phosphate-]n of N. meningitidis serogroup A, one of the six serogroups (A, B, C, W-135, X, and Y) that account for most cases of Neisseria meningitidis-caused bacterial septicemia and meningitis
physiological function
-
UDP-GlcNAc 2-epimerase catalyzes the interconversion of UDP-GlcNAc to UDP-ManNAc, which is used in the biosynthesis of cell surface polysaccharides in bacteria
-
physiological function
Neisseria meningitidis serogroup A / serotype 4A Z2491
-
SacA is proposed to be involved in the first step in serogroup A capsular polysaccharides (CPS) biosynthetic pathway and is critical for serogroup A CPS biosynthesis. It catalyzes the interconversion between UDP-GlcNAc and UDP-ManNAc. This epimerization process is independent of nicotinamide adenine dinucleotide oxidized form (NAD+) and is critical for synthesizing bacterial ManNAc-containing CPSs
-
physiological function
Neisseria meningitidis serogroup A /serotype 4A Z2491
-
Neisseria meningitidis serogroup A non-hydrolyzing UDP-GlcNAc 2-epimerase (NmSacA) catalyzes the interconversion between UDP-GlcNAc and uridine 5?-diphosphate-N-acetylmannosamine (UDP-ManNAc). It is a key enzyme involved in the biosynthesis of the capsular polysaccharide [-6ManNAc?1-phosphate-]n of N. meningitidis serogroup A, one of the six serogroups (A, B, C, W-135, X, and Y) that account for most cases of Neisseria meningitidis-caused bacterial septicemia and meningitis
-
physiological function
-
2-epimerase MnaA interconverts UDP-GlcNAc and UDP-ManNAc to modulate substrate levels of TarO and TarA wall teichoic acid (WTA) biosynthesis enzymes. Besides MnaA, Staphylococcus aureus maintains a second 2-epimerase involved in serotype 5 capsular polysaccharide (CP5) synthesis, Cap5P. MnaA and Cap5P provide compensatory WTA functional roles in Staphylococcus aureus. MnaA and other enzymes of WTA biosynthesis are required for biofilm formation in MRSA. Overlapping functional activity of MnaA and Cap5P in Staphylococci
-
physiological function
-
2-epimerase MnaA interconverts UDP-GlcNAc and UDP-ManNAc to modulate substrate levels of TarO and TarA wall teichoic acid (WTA) biosynthesis enzymes. MnaA serves as the sole 2-epimerase required for WTA biosynthesis in Staphylococcus epidermidis. MnaA and other enzymes of WTA biosynthesis are required for biofilm formation in MRSE
-
additional information
a comparison of the crystal structures in open and closed conformations shows that upon UDP and UDPGlcNAc binding, the enzyme undergoes conformational changes involving a rigid-body movement of the C-terminal domain. Comparison of the crystal structures of Methanocaldococcus jannaschii and of Bacillus subtilis. Structural superimposition of closed-form and open-form Mj-epimerase. Homologous enzyme structure comparisons, overview
additional information
-
a comparison of the crystal structures in open and closed conformations shows that upon UDP and UDPGlcNAc binding, the enzyme undergoes conformational changes involving a rigid-body movement of the C-terminal domain. Comparison of the crystal structures of Methanocaldococcus jannaschii and of Bacillus subtilis. Structural superimposition of closed-form and open-form Mj-epimerase. Homologous enzyme structure comparisons, overview
additional information
comparison of the crystal structures of Methanocaldococcus jannaschii in open and closed conformations and of Bacillus subtilis. Homologous enzyme structure comparisons, overview
additional information
-
comparison of the crystal structures of Methanocaldococcus jannaschii in open and closed conformations and of Bacillus subtilis. Homologous enzyme structure comparisons, overview
additional information
Neisseria meningitidis serogroup A / serotype 4A
of the six major disease-causing Neisseria meningitidis serogroups, only serogroups A and X produce capsular polysaccharides (CPSs) that do not have N-acetylneuraminic acid (Neu5Ac, sialic acid is a more general term) residues. Unlike the CPSs of serogroups B and C which are homopolymers of Neu5Ac with alpha2-8- and alpha2-9-linkages respectively, or serogroups W-135 and Y CPSs which are heteropolymers of [-6Gal/Glcalpha1-4Neu5Acalpha2-]n with alternating Neu5Ac and Gal/Glc as disaccharide repeating units, the CPS of serogroup A is a homopolymer of [-6ManNAcalpha1-phosphate-]n. Correspondingly, the genetic organization for serogroup A capsule is different from those for serogroups B, C, W-135, and Y
additional information
Neisseria meningitidis serogroup A /serotype 4A
homology modeling and molecular docking reveal structural determinants of NmSacA substrate specificity. Disulfide bond formation is not required for the epimerase activity of NmSacA-His6
additional information
-
comparison of the crystal structures of Methanocaldococcus jannaschii in open and closed conformations and of Bacillus subtilis. Homologous enzyme structure comparisons, overview
-
additional information
Neisseria meningitidis serogroup A / serotype 4A Z2491
-
of the six major disease-causing Neisseria meningitidis serogroups, only serogroups A and X produce capsular polysaccharides (CPSs) that do not have N-acetylneuraminic acid (Neu5Ac, sialic acid is a more general term) residues. Unlike the CPSs of serogroups B and C which are homopolymers of Neu5Ac with alpha2-8- and alpha2-9-linkages respectively, or serogroups W-135 and Y CPSs which are heteropolymers of [-6Gal/Glcalpha1-4Neu5Acalpha2-]n with alternating Neu5Ac and Gal/Glc as disaccharide repeating units, the CPS of serogroup A is a homopolymer of [-6ManNAcalpha1-phosphate-]n. Correspondingly, the genetic organization for serogroup A capsule is different from those for serogroups B, C, W-135, and Y
-
additional information
Neisseria meningitidis serogroup A /serotype 4A Z2491
-
homology modeling and molecular docking reveal structural determinants of NmSacA substrate specificity. Disulfide bond formation is not required for the epimerase activity of NmSacA-His6
-
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H242A
-
dramatic decrease in catalytic efficiency
H44Q
-
dramatic decrease in catalytic efficiency
Q43A
-
dramatic decrease in catalytic efficiency
Q70A
-
dramatic decrease in catalytic efficiency
R210A
-
dramatic decrease in catalytic efficiency
C303V
exhibited almost no reduction in epimerase activity
C303X
the C303X protein does not display any enzymatic activity
D378Y
60% reduction of epimerase activity
D95N
-
about 18000 fold decrease in turnover number for UDP-N-acetyl-D-glucosamine, not possible to obtain accurate kinetic constants
E117Q
-
about 18000 fold decrease in turnover number for UDP-N-acetyl-D-glucosamine, not possible to obtain accurate kinetic constants
E131Q
-
about 18000 fold decrease in turnover number for UDP-N-acetyl-D-glucosamine, not possible to obtain accurate kinetic constants
H213N
-
30fold increase in Km-value and 50fold decrease in turnover-number for UDP-N-acetyl-D-glucosamine. Unlike the wild-type enzyme no inhibition is detected at UDP-concentrations up to 10 mM
I200F
exhibited almost no reduction in epimerase activity
K15A
-
more than 100fold increase in KM-value for UDP-N-acetyl-D-glucosamine
A630T
-
mutation in patients with distal myopathy with rimmed vacuoles, UDP-N-acetylglucosamine 2-epimerase activity of mutant enzyme is reduced to 70-80% of wild-type activity
A631V
-
a naturally occuring missense mutation in exon 11 of the GNE gene of a patient with hereditary inclusion body myopathy
C303V
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
C303X
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
D177C
-
mutation in patients with distal myopathy with rimmed vacuoles, UDP-N-acetylglucosamine 2-epimerase activity of mutant enzyme is reduced to less than 20% of wild-type
D225N
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
E2G
-
a naturally occuring missense mutation in exon 2 of the GNE gene of a patient with hereditary inclusion body myopathy
G135V
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
G135V/R246W
-
mutation in patients with hereditary inclusion body myopathy: G135V/R246W (GNE/GNE domain mutation), UDP-N-acetylglucosamine 2-epimerase activity is 38% of wild-type, N-acetylmannosamine kinase activity is 72% of wild-type
G206S
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
G708S
-
mutation in patients with distal myopathy with rimmed vacuoles, UDP-N-acetylglucosamine 2-epimerase activity of mutant enzyme is reduced to 50% of wild-type activity
G89R
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
I142T
-
a naturally occuring missense mutation in exon 3 of the GNE gene of a patient with hereditary inclusion body myopathy
I200F
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
I241S
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
I298T
-
a naturally occuring missense mutation in exon 5 of the GNE gene of a patient with hereditary inclusion body myopathy
I472T
-
mutation in patients with distal myopathy with rimmed vacuoles, UDP-N-acetylglucosamine 2-epimerase activity of mutant enzyme is reduced to 50% of wild-type activity
L379H
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
L556S
-
a naturally occuring missense mutation in exon 10 of the GNE gene of a patient with hereditary inclusion body myopathy
M171V
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
M29T
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
M712T/M712T
-
M712T/M712T (MNK/MNK domain mutation), UDP-N-acetylglucosamine 2-epimerase activity is 83% of wild-type, N-acetylmannosamine kinase activity is 55% of wild-type
P27S
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
P283S
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
P36L
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
Q436X
-
a naturally occuring nonsense mutation in exon 8 of the GNE gene of a patient with hereditary inclusion body myopathy
R11W
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
R129Q
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
R162C
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
R177C
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
R202L
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
R246W
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
R263L
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
R277C
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
R306Q
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
R71W
-
a naturally occuring missense mutation in exon 3 of the GNE gene of a patient with hereditary inclusion body myopathy
R8X
-
a naturally occuring nonsense mutation in exon 2 of the GNE gene of a patient with hereditary inclusion body myopathy
S615X
-
a naturally occuring nonsense mutation in exon 11 of the GNE gene of a patient with hereditary inclusion body myopathy
V216A
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
V216A/A631V
-
V216A/A631V (GNE/MNK domain mutation), UDP-N-acetylglucosamine 2-epimerase activity is 48% of wild-type, N-acetylmannosamine kinase activity is 63% of wild-type
V367I
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
V572L
-
mutation in patients with distal myopathy with rimmed vacuoles, UDP-N-acetylglucosamine 2-epimerase activity of mutant enzyme is reduced to 70-80% of wild-type activity
W204X
-
a naturally occuring nonsense mutation in exon 3 of the GNE gene of a patient with hereditary inclusion body myopathy
Y675H
-
a naturally occuring missense mutation in exon 12 of the GNE gene of a patient with hereditary inclusion body myopathy
D100N
-
no conversion of UDP-N-acetyl-D-glucosamine to UDP + N-acetyl-D-mannosamine
D131N
-
no conversion of UDP-N-acetyl-D-glucosamine to UDP + N-acetyl-D-mannosamine, acetamidoglucal is released from the active site during catalysis
E122Q
-
no conversion of UDP-N-acetyl-D-glucosamine to UDP + N-acetyl-D-mannosamine, acetamidoglucal is released from the active site during catalysis
D100N
-
no conversion of UDP-N-acetyl-D-glucosamine to UDP + N-acetyl-D-mannosamine
-
D131N
-
no conversion of UDP-N-acetyl-D-glucosamine to UDP + N-acetyl-D-mannosamine, acetamidoglucal is released from the active site during catalysis
-
E122Q
-
no conversion of UDP-N-acetyl-D-glucosamine to UDP + N-acetyl-D-mannosamine, acetamidoglucal is released from the active site during catalysis
-
D413K
-
enzyme with mutation in the putative kinase active site shows drastic loss in their kinase activity but retains their epimerase activity
D413N
-
enzyme with mutation in the putative kinase active site shows drastic loss in their kinase activity but retains their epimerase activity
DELTA1-234
-
mutant enzyme shows no N-epimerase activity
DELTA1-356
-
mutant enzyme shows no N-epimerase activity
DELTA1-39
-
mutant enzyme shows no N-epimerase activity
DELTA383-722
-
epimerase activity is 2% of wild-type enzyme
DELTA490-722
-
epimerase activity is 15% of wild-type enzyme
DELTA597-722
-
epimerase activity is 2% of wild-type enzyme
DELTA697-722
-
epimerase activity is about 70% of wild-type enzyme
DELTA717-722
-
epimerase activity is about 95% of wild-type enzyme
H110A
-
mutant enzyme shows a drastic loss of epimerase activity, oligomerization is significantly different from that of the wild-type enzyme,loss of epimerase activity can largely by attributed to incorrect protein folding
H132A
-
mutant enzyme shows a drastic loss of epimerase activity, oligomerization is significantly different from that of the wild-type enzyme, loss of epimerase activity can largely by attributed to incorrect protein folding
H45A
-
mutant enzyme shows a drastic loss of epimerase activity
R420M
-
enzyme with mutation in the putative kinase active site shows drastic loss in their kinase activity but retains their epimerase activity
P12L
site-diected mutagenesis
Y194X
site-directed mutagenesis
P12L
-
site-diected mutagenesis
-
Y194X
-
site-directed mutagenesis
-
C13S
-
mutation in patients with distal myopathy with rimmed vacuoles, UDP-N-acetylglucosamine 2-epimerase activity of mutant enzyme is reduced to less than 20% of wild-type
C13S
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
D176V
-
mutation in patients with distal myopathy with rimmed vacuoles, UDP-N-acetylglucosamine 2-epimerase activity of mutant enzyme is reduced to less than 20% of wild-type
D176V
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
D378Y
-
mutation in patients with distal myopathy with rimmed vacuoles, UDP-N-acetylglucosamine 2-epimerase activity of mutant enzyme is reduced to less than 20% of wild-type
D378Y
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
H132Q
-
mutation in patients with distal myopathy with rimmed vacuoles, UDP-N-acetylglucosamine 2-epimerase activity of mutant enzyme is reduced to less than 20% of wild-type
H132Q
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
M712T
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
M712T
the Persian-Jewish HIBM founder mutation is located at the interface alpha4alpha10 of GNE and likely affects GlcNAc, Mg2+, and ATP binding
R246Q
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
R246Q
-
a naturally occuring missense mutation in exon 4 of the GNE gene of a patient with hereditary inclusion body myopathy
R266Q
-
GNE mutants are created by site-directed mutagenesis with the mutagenic oligonucleotides 5'-GGTTCGAGTGATGCAGAAGAAGGGCATTGAGCA-3' for the R266Q sialuria mutations (where the site of mutation is underlined) through PCR-like amplification with Pfu polymerase.
R266Q
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
R266W
-
GNE mutants are created by site-directed mutagenesis with the mutagenic oligonucleotides 5'-GGTTCGAGTGATGTGGAAGAAGGGCATTGAGCA-3' for the R266W sialuria mutations (where the site of mutation is underlined) through PCR-like amplification with Pfu polymerase.
R266W
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
R335W
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
R335W
-
a naturally occuring missense mutation in exon 6 of the GNE gene of a patient with hereditary inclusion body myopathy
V331A
-
mutation in patients with distal myopathy with rimmed vacuoles, UDP-N-acetylglucosamine 2-epimerase activity of mutant enzyme is reduced to less than 20% of wild-type
V331A
a naturally occuirng missense mutation the epimerase part of the bifunctional enzyme
V696M
-
a naturally occuring missense mutation in exon 12 of the GNE gene of a patient with hereditary inclusion body myopathy
V696M
-
naturally occuring missense mutation G2086A involved in hereditary inclusion body myopathy, phenotype, overview
H155A
-
mutant enzyme forms mainly trimeric enzyme with small amounts of hexamer
H155A
-
mutant enzyme shows a drastic loss of epimerase activity, loss of epimerase activity can largely by attributed to incorrect protein folding
H157A
-
mutant enzyme forms mainly trimeric enzyme with small amounts of hexamer
H157A
-
mutant enzyme shows a drastic loss of epimerase activity, loss of epimerase activity can largely by attributed to incorrect protein folding
additional information
-
splice variant hGNE2, recombinantly expressed in insect and mamalian cells, displays selective reduction of UDPGlcNAc 2-epimerase activity by the loss of its tetrameric state, which is essential for full enzyme activity. Splice variant hGNE3 only possesses kinase activity
additional information
-
a synonymous variation, p.Y591Y, codon tac>tat, is seen in a patient bearing compound heterozygous nonsynonymous mutation, p.S615X and p.Y675H
additional information
mutant genotyping, overview. Modeling of effects of GNE/MNK missense mutations associated with HIBM or sialuria on helix arrangement, substrate binding, and enzyme action, overview. All reported mutations are associated with the active sites or secondary structure interfaces of GNE/MNK
additional information
-
mutant genotyping, overview. Modeling of effects of GNE/MNK missense mutations associated with HIBM or sialuria on helix arrangement, substrate binding, and enzyme action, overview. All reported mutations are associated with the active sites or secondary structure interfaces of GNE/MNK
additional information
-
sialuria is caused by the loss of feedback control of UDP-GlcNAc 2-epimerase activity due to the mutation of only one of the two arginine residues 263 and 266
additional information
-
the frame shif mutation 1295delA, leading to a premature stop codon at K432, is involved in hereditary inclusion body myopathy, phenotype, overview
additional information
-
transgenic Arabidopsis thaliana plants expressing three key enzymes of the mammalian Neu5Ac biosynthesis pathway: UDPN-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, N-acetylneuraminic acid phosphate synthase, and CMP-Nacetylneuraminic acid synthetase. Simultaneous expression of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase and N-acetylneuraminic acid phosphate synthase results in the generation of significant Neu5Ac amounts of 1275 nmol per g fresh weight in leaves, which can be further converted to cytidine monophospho-N-acetylneuraminic acid by coexpression of CMP-N-acetylneuraminic acid synthetase
additional information
-
generation of GNE knockout mice by gene targeting, enzyme knockout leads to embryonic lethality, phenotype, overview. Impaired sialylation of glycoconjugates induces cell death, either by the loss of the sialic acid specific masking of cells to prevent proteolytic attack or by the prevention of cell migration and differentiation
additional information
gene mnaA, genotyping and mutation identification. Mapping of MnaA LOF mutations into the MnaA crystal structure revealing key residues for substrate binding site stability and charge. To determine whether L638R mnaA LOF mutants are not identified in MRSA COL due to a functional redundancy between Cap5P and MnaA, a cap5P deletion mutant is constructed and the L638R studies are repeated. Under these conditions, in addition to identifying the expected tarG L638R mutations as well as tarO and tarA LOF mutations, multiple (n = 11) independent resistor isolates obtained uniquely possess distinct mutations that map to mnaA and are predicted to inactivate gene function as well as directly confer L638R drug resistance based on the absence of additional non-synonymous mutations in their genome following WGS analysis. While MRSA COL DELTAcap5P exhibits no wall teichoic acid (WTA) depletion phenotype and remains resistant to beta-lactams, MRSA COL mnaA, DELTAcap5P double mutants are completely devoid of WTA and are also highly sensitive to beta-lactams. MRSA COL mnaA, cap5P double mutants and MRSE mnaA single mutants reveal morphological phenotypes consistent with WTA depletion, including increased cell size heterogeneity and septation defects. Complementing DELTAcap5P mnaASa P12L and DELTAcap5P mnaASa Y194* with either cap5P or mnaASa reintroduced on an inducible plasmid restores WTA polymer levels, resistance to each of the beta-lactams tested, and wild-type sensitivity to L638
additional information
gene mnaA, genotyping and mutation identification. Mapping of MnaA LOF mutations into the MnaA crystal structure revealing key residues for substrate binding site stability and charge. To determine whether L638R mnaA LOF mutants are not identified in MRSA COL due to a functional redundancy between Cap5P and MnaA, a cap5P deletion mutant is constructed and the L638R studies are repeated. Under these conditions, in addition to identifying the expected tarG L638R mutations as well as tarO and tarA LOF mutations, multiple (n = 11) independent resistor isolates obtained uniquely possess distinct mutations that map to mnaA and are predicted to inactivate gene function as well as directly confer L638R drug resistance based on the absence of additional non-synonymous mutations in their genome following WGS analysis. While MRSA COL DELTAcap5P exhibits no wall teichoic acid (WTA) depletion phenotype and remains resistant to beta-lactams, MRSA COL mnaA, DELTAcap5P double mutants are completely devoid of WTA and are also highly sensitive to beta-lactams. MRSA COL mnaA, cap5P double mutants and MRSE mnaA single mutants reveal morphological phenotypes consistent with WTA depletion, including increased cell size heterogeneity and septation defects. Complementing DELTAcap5P mnaASa P12L and DELTAcap5P mnaASa Y194* with either cap5P or mnaASa reintroduced on an inducible plasmid restores WTA polymer levels, resistance to each of the beta-lactams tested, and wild-type sensitivity to L638
additional information
-
gene mnaA, genotyping and mutation identification. Mapping of MnaA LOF mutations into the MnaA crystal structure revealing key residues for substrate binding site stability and charge. To determine whether L638R mnaA LOF mutants are not identified in MRSA COL due to a functional redundancy between Cap5P and MnaA, a cap5P deletion mutant is constructed and the L638R studies are repeated. Under these conditions, in addition to identifying the expected tarG L638R mutations as well as tarO and tarA LOF mutations, multiple (n = 11) independent resistor isolates obtained uniquely possess distinct mutations that map to mnaA and are predicted to inactivate gene function as well as directly confer L638R drug resistance based on the absence of additional non-synonymous mutations in their genome following WGS analysis. While MRSA COL DELTAcap5P exhibits no wall teichoic acid (WTA) depletion phenotype and remains resistant to beta-lactams, MRSA COL mnaA, DELTAcap5P double mutants are completely devoid of WTA and are also highly sensitive to beta-lactams. MRSA COL mnaA, cap5P double mutants and MRSE mnaA single mutants reveal morphological phenotypes consistent with WTA depletion, including increased cell size heterogeneity and septation defects. Complementing DELTAcap5P mnaASa P12L and DELTAcap5P mnaASa Y194* with either cap5P or mnaASa reintroduced on an inducible plasmid restores WTA polymer levels, resistance to each of the beta-lactams tested, and wild-type sensitivity to L638
additional information
to determine whether L638R mnaA LOF mutants are not identified in MRSA COL due to a functional redundancy between Cap5P and MnaA, a cap5P deletion mutant is constructed and the L638R studies are repeated. Under these conditions, in addition to identifying the expected tarG L638R mutations as well as tarO and tarA LOF mutations, multiple (n = 11) independent resistor isolates obtained uniquely possess distinct mutations that map to mnaA and are predicted to inactivate gene function as well as directly confer L638R drug resistance based on the absence of additional non-synonymous mutations in their genome following WGS analysis. While MRSA COL DELTAcap5P exhibits no wall teichoic acid (WTA) depletion phenotype and remains resistant to beta-lactams, MRSA COL mnaA, DELTAcap5P double mutants are completely devoid of WTA and are also highly sensitive to beta-lactams. MRSA COL mnaA, cap5P double mutants and MRSE mnaA single mutants reveal morphological phenotypes consistent with WTA depletion, including increased cell size heterogeneity and septation defects
additional information
to determine whether L638R mnaA LOF mutants are not identified in MRSA COL due to a functional redundancy between Cap5P and MnaA, a cap5P deletion mutant is constructed and the L638R studies are repeated. Under these conditions, in addition to identifying the expected tarG L638R mutations as well as tarO and tarA LOF mutations, multiple (n = 11) independent resistor isolates obtained uniquely possess distinct mutations that map to mnaA and are predicted to inactivate gene function as well as directly confer L638R drug resistance based on the absence of additional non-synonymous mutations in their genome following WGS analysis. While MRSA COL DELTAcap5P exhibits no wall teichoic acid (WTA) depletion phenotype and remains resistant to beta-lactams, MRSA COL mnaA, DELTAcap5P double mutants are completely devoid of WTA and are also highly sensitive to beta-lactams. MRSA COL mnaA, cap5P double mutants and MRSE mnaA single mutants reveal morphological phenotypes consistent with WTA depletion, including increased cell size heterogeneity and septation defects
additional information
-
to determine whether L638R mnaA LOF mutants are not identified in MRSA COL due to a functional redundancy between Cap5P and MnaA, a cap5P deletion mutant is constructed and the L638R studies are repeated. Under these conditions, in addition to identifying the expected tarG L638R mutations as well as tarO and tarA LOF mutations, multiple (n = 11) independent resistor isolates obtained uniquely possess distinct mutations that map to mnaA and are predicted to inactivate gene function as well as directly confer L638R drug resistance based on the absence of additional non-synonymous mutations in their genome following WGS analysis. While MRSA COL DELTAcap5P exhibits no wall teichoic acid (WTA) depletion phenotype and remains resistant to beta-lactams, MRSA COL mnaA, DELTAcap5P double mutants are completely devoid of WTA and are also highly sensitive to beta-lactams. MRSA COL mnaA, cap5P double mutants and MRSE mnaA single mutants reveal morphological phenotypes consistent with WTA depletion, including increased cell size heterogeneity and septation defects
additional information
-
to determine whether L638R mnaA LOF mutants are not identified in MRSA COL due to a functional redundancy between Cap5P and MnaA, a cap5P deletion mutant is constructed and the L638R studies are repeated. Under these conditions, in addition to identifying the expected tarG L638R mutations as well as tarO and tarA LOF mutations, multiple (n = 11) independent resistor isolates obtained uniquely possess distinct mutations that map to mnaA and are predicted to inactivate gene function as well as directly confer L638R drug resistance based on the absence of additional non-synonymous mutations in their genome following WGS analysis. While MRSA COL DELTAcap5P exhibits no wall teichoic acid (WTA) depletion phenotype and remains resistant to beta-lactams, MRSA COL mnaA, DELTAcap5P double mutants are completely devoid of WTA and are also highly sensitive to beta-lactams. MRSA COL mnaA, cap5P double mutants and MRSE mnaA single mutants reveal morphological phenotypes consistent with WTA depletion, including increased cell size heterogeneity and septation defects
-
additional information
-
gene mnaA, genotyping and mutation identification. Mapping of MnaA LOF mutations into the MnaA crystal structure revealing key residues for substrate binding site stability and charge. To determine whether L638R mnaA LOF mutants are not identified in MRSA COL due to a functional redundancy between Cap5P and MnaA, a cap5P deletion mutant is constructed and the L638R studies are repeated. Under these conditions, in addition to identifying the expected tarG L638R mutations as well as tarO and tarA LOF mutations, multiple (n = 11) independent resistor isolates obtained uniquely possess distinct mutations that map to mnaA and are predicted to inactivate gene function as well as directly confer L638R drug resistance based on the absence of additional non-synonymous mutations in their genome following WGS analysis. While MRSA COL DELTAcap5P exhibits no wall teichoic acid (WTA) depletion phenotype and remains resistant to beta-lactams, MRSA COL mnaA, DELTAcap5P double mutants are completely devoid of WTA and are also highly sensitive to beta-lactams. MRSA COL mnaA, cap5P double mutants and MRSE mnaA single mutants reveal morphological phenotypes consistent with WTA depletion, including increased cell size heterogeneity and septation defects. Complementing DELTAcap5P mnaASa P12L and DELTAcap5P mnaASa Y194* with either cap5P or mnaASa reintroduced on an inducible plasmid restores WTA polymer levels, resistance to each of the beta-lactams tested, and wild-type sensitivity to L638
-
additional information
-
gene mnaA, genotyping and mutation identification. MRSA COL mnaA, cap5P double mutants and MRSE mnaA single mutants reveal morphological phenotypes consistent with WTA depletion, including increased cell size heterogeneity and septation defects
additional information
-
gene mnaA, genotyping and mutation identification. MRSA COL mnaA, cap5P double mutants and MRSE mnaA single mutants reveal morphological phenotypes consistent with WTA depletion, including increased cell size heterogeneity and septation defects
-
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Spivak, C.T.; Roseman, S.
UDP-N-acetyl-D-glucosamine 2'-epimerase
Methods Enzymol.
9
612-615
1966
Rattus norvegicus
-
brenda
Salo, W.L.; Fletcher, H.G.
Studies on the mechanism of action of uridine diphosphate N-acetylglucosamine 2-epimerase
Biochemistry
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882-885
1970
Rattus norvegicus
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Sommar, K.M.; Ellis, D.B.
Uridine diphosphate N-acetyl-D-glucosamine 2-epimerase from rat liver. I. Catalytic and regulatory properties
Biochim. Biophys. Acta
268
581-589
1972
Rattus norvegicus
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Sommar, K.M.; Ellis, D.B.
Uridine diphosphate N-acetyl-D-glucosamine 2-epimerase from rat liver. II. Studies on the mechanism of action
Biochim. Biophys. Acta
268
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1972
Rattus norvegicus
brenda
Kikuchi, K.; Tsuiki, S.
Purification and properties of UDP-N-acetylglucosamine 2'-epimerase from rat liver
Biochim. Biophys. Acta
327
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1973
Rattus norvegicus
brenda
Kawamura, T.; Ichihara, N.; Ishimoto, N.; Ito, E.
Biosynthesis of uridine diphosphate N-acetyl-D-mannosaminuronic acid from uridine diphosphate N-acetyl-D-glucosamine in Escherichia coli: separation of enzymes responsible for epimerization and dehydrogenation
Biochem. Biophys. Res. Commun.
66
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1975
Escherichia coli
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The incorporation of tritium from tritium-enriched water into UDP-N-acetylglucosamine and UDP-N-acetyl-mannosamine catalyzed by UDP-N-acetylglucosamine 2-epimerase from Escherichia coli
Biochim. Biophys. Acta
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1976
Escherichia coli
brenda
Kawamura, T.; Kimura, M.; Yamamori, S.; Ito, E.
Enzymatic formation of uridine diphosphate N-acetyl-D-mannosamine
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253
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1978
Bacillus cereus, Priestia megaterium, Bacillus subtilis, Escherichia coli, Micrococcus luteus, Staphylococcus aureus
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Enzymatic synthesis of uridine diphosphate N-acetyl-D-mannosaminuronic acid
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Escherichia coli
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Rattus norvegicus
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UDP-N-acetylglucosamine 2'-epimerase of rat hepatoma and its comparison with the enzyme of rat liver
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1980
Mus musculus, Rattus norvegicus
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UDP-N-acetyl-D-glucosamine 2'-epimerase from Escherichia coli
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1983
Rattus norvegicus
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Inhibition of the biosynthesis of N-acetylneuraminic acid by metal ions and selenium in vitro
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Overexpression, purification, crystallization and data collection on the Bordetella pertussis wlbD gene product, a putative UDP-GlcNAc 2'-epimerase
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The structure of UDP-N-acetylglucosamine 2-epimerase reveals homology to phosphoglycosyl transferases
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The NeuC protein of Escherichia coli K1 is a UDP N-acetylglucosamine 2-epimerase
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Homo sapiens
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2004
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Murkin, A.S.; Chou, W.K.; Wakarchuk, W.W.; Tanner, M.E.
Identification and mechanism of a bacterial hydrolyzing UDP-N-acetylglucosamine 2-epimerase
Biochemistry
43
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2004
Neisseria meningitidis
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Samuel, J.; Tanner, M.E.
Active site mutants of the "non-hydrolyzing" UDP-N-acetylglucosamine 2-epimerase from Escherichia coli
Biochim. Biophys. Acta
1700
85-91
2004
Escherichia coli
brenda
Krause, S.; Hinderlich, S.; Amsili, S.; Horstkorte, R.; Wiendl, H.; Argov, Z.; Mitrani-Rosenbaum, S.; Lochmueller, H.
Localization of UDP-GlcNAc 2-epimerase/ManAc kinase (GNE) in the Golgi complex and the nucleus of mammalian cells
Exp. Cell Res.
304
365-379
2005
Homo sapiens
brenda
Giordanengo, V.; Ollier, L.; Lanteri, M.; Lesimple, J.; March, D.; Thyss, S.; Lefebvre, J.C.
Epigenetic reprogramming of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) in HIV-1-infected CEM T cells
FASEB J.
18
1961-1963
2004
Homo sapiens (Q9Y223)
brenda
Hinderlich, S.; Salama, I.; Eisenberg, I.; Potikha, T.; Mantey, L.R.; Yarema, K.J.; Horstkorte, R.; Argov, Z.; Sadeh, M.; Reutter, W.; Mitrani-Rosenbaum, S.
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
FEBS Lett.
566
105-109
2004
Homo sapiens (Q9Y223), Homo sapiens
brenda
Sparks, S.E.; Ciccone, C.; Lalor, M.; Orvisky, E.; Klootwijk, R.; Savelkoul, P.J.; Dalakas, M.C.; Krasnewich, D.M.; Gahl, W.A.; Huizing, M.
Use of a cell-free system to determine UDP-N-acetylglucosamine 2-epimerase and N-acetylmannosamine kinase activities in human hereditary inclusion body myopathy
Glycobiology
15
1102-1110
2005
Homo sapiens
brenda
Noguchi, S.; Keira, Y.; Murayama, K.; Ogawa, M.; Fujita, M.; Kawahara, G.; Oya, Y.; Imazawa, M.; Goto, Y.I.; Hayashi, Y.K.; Nonaka, I.; Nishino, I.
Reduction of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase activity and sialylation in distal myopathy with rimmed vacuoles
J. Biol. Chem.
279
11402-11407
2004
Homo sapiens
brenda
Blume, A.; Benie, A.J.; Stolz, F.; Schmidt, R.R.; Reutter, W.; Hinderlich, S.; Peters, T.
Characterization of ligand binding to the bifunctional key enzyme in the sialic acid biosynthesis by NMR: I. Investigation of the UDP-GlcNAc 2-epimerase functionality
J. Biol. Chem.
279
55715-55721
2004
Rattus norvegicus
brenda
Blume, A.; Ghaderi, D.; Liebich, V.; Hinderlich, S.; Donner, P.; Reutter, W.; Lucka, L.
UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, functionally expressed in and purified from Escherichia coli, yeast, and insect cells
Protein Expr. Purif.
35
387-396
2004
Rattus norvegicus
brenda
Penner, J.; Mantey, L.R.; Elgavish, S.; Ghaderi, D.; Cirak, S.; Berger, M.; Krause, S.; Lucka, L.; Voit, T.; Mitrani-Rosenbaum, S.; Hinderlich, S.
Influence of UDP-GlcNAc 2-epimerase/ManNAc kinase mutant proteins on hereditary inclusion body myopathy
Biochemistry
45
2968-2977
2006
Escherichia coli (P27828), Escherichia coli
brenda
Reinke, S.O.; Hinderlich, S.
Prediction of three different isoforms of the human UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
FEBS Lett.
581
3327-3331
2007
Mus musculus (Q3UW64), Homo sapiens (Q9Y223), Homo sapiens
brenda
Bork, K.; Reutter, W.; Weidemann, W.; Horstkorte, R.
Enhanced sialylation of EPO by overexpression of UDP-GlcNAc 2-epimerase/ManAc kinase containing a sialuria mutation in CHO cells
FEBS Lett.
581
4195-4198
2007
Rattus norvegicus
brenda
Gagiannis, D.; Orthmann, A.; Danssmann, I.; Schwarzkopf, M.; Weidemann, W.; Horstkorte, R.
Reduced sialylation status in UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase (GNE)-deficient mice
Glycoconj. J.
24
125-130
2007
Mus musculus
brenda
Wang, Z.; Sun, Z.; Li, A.V.; Yarema, K.J.
Roles for UDP-GlcNAc 2-epimerase/ManNAc 6-kinase outside of sialic acid biosynthesis: modulation of sialyltransferase and BiP expression, GM3 and GD3 biosynthesis, proliferation, and apoptosis, and ERK1/2 phosphorylation
J. Biol. Chem.
281
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2006
Homo sapiens
brenda
Ghaderi, D.; Strauss, H.M.; Reinke, S.; Cirak, S.; Reutter, W.; Lucka, L.; Hinderlich, S.
Evidence for dynamic interplay of different oligomeric states of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase by biophysical methods
J. Mol. Biol.
369
746-758
2007
Rattus norvegicus
brenda
Castilho, A.; Pabst, M.; Leonard, R.; Veit, C.; Altmann, F.; Mach, L.; Gloessl, J.; Strasser, R.; Steinkellner, H.
Construction of a functional CMP-sialic acid biosynthesis pathway in Arabidopsis
Plant Physiol.
147
331-339
2008
Mus musculus
brenda
Velloso, L.M.; Bhaskaran, S.S.; Schuch, R.; Fischetti, V.A.; Stebbins, C.E.
A structural basis for the allosteric regulation of non-hydrolysing UDP-GlcNAc 2-epimerases. [Erratum to document cited in CA148:302197]
EMBO Rep.
9
1251
2008
Bacillus anthracis
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brenda
Reinke, S.O.; Eidenschink, C.; Jay, C.M.; Hinderlich, S.
Biochemical characterization of human and murine isoforms of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE)
Glycoconj. J.
26
415-422
2009
Homo sapiens, Mus musculus
brenda
Namboori, S.C.; Graham, D.E.
Acetamido sugar biosynthesis in the Euryarchaea
J. Bacteriol.
190
2987-2996
2008
Methanococcus maripaludis (Q6LZC4)
brenda
Amsili, S.; Zer, H.; Hinderlich, S.; Krause, S.; Becker-Cohen, M.; MacArthur, D.G.; North, K.N.; Mitrani-Rosenbaum, S.
UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) binds to alpha-actinin 1: novel pathways in skeletal muscle?
PLoS ONE
3
e2477
2008
Homo sapiens
brenda
Reinke, S.O.; Lehmer, G.; Hinderlich, S.; Reutter, W.
Regulation and pathophysiological implications of UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE) as the key enzyme of sialic acid biosynthesis
Biol. Chem.
390
591-599
2009
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Voermans, N.C.; Guillard, M.; Doedee, R.; Lammens, M.; Huizing, M.; Padberg, G.W.; Wevers, R.A.; van Engelen, B.G.; Lefeber, D.J.
Clinical features, lectin staining, and a novel GNE frameshift mutation in hereditary inclusion body myopathy
Clin. Neuropathol.
29
71-77
2010
Homo sapiens
brenda
Saechao, C.; Valles-Ayoub, Y.; Esfandiarifard, S.; Haghighatgoo, A.; No, D.; Shook, S.; Mendell, J.R.; Rosales-Quintero, X.; Felice, K.J.; Morel, C.F.; Pietruska, M.; Darvish, D.
Novel GNE mutations in hereditary inclusion body myopathy patients of non-Middle Eastern descent
Genet. Test. Mol. Biomarkers
14
157-162
2010
Homo sapiens
brenda
Weidemann, W.; Klukas, C.; Klein, A.; Simm, A.; Schreiber, F.; Horstkorte, R.
Lessons from GNE-deficient embryonic stem cells: sialic acid biosynthesis is involved in proliferation and gene expression
Glycobiology
20
107-117
2010
Mus musculus
brenda
Kurochkina, N.; Yardeni, T.; Huizing, M.
Molecular modeling of the bifunctional enzyme UDP-GlcNAc 2-epimerase/ManNAc kinase and predictions of structural effects of mutations associated with HIBM and sialuria
Glycobiology
20
322-337
2010
Homo sapiens (Q9Y223), Homo sapiens
brenda
Moeller, H.; Boehrsch, V.; Lucka, L.; Hackenberger, C.P.; Hinderlich, S.
Efficient metabolic oligosaccharide engineering of glycoproteins by UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) knock-down
Mol. Biosyst.
7
2245-2251
2011
Homo sapiens
brenda
Xu, Y.; Brenning, B.; Clifford, A.; Vollmer, D.; Bearss, J.; Jones, C.; McCarthy, V.; Shi, C.; Wolfe, B.; Aavula, B.; Warner, S.; Bearss, D.J.; McCullar, M.V.; Schuch, R.; Pelzek, A.; Bhaskaran, S.S.; Stebbins, C.E.; Goldberg, A.R.; Fischetti, V.A.; Vankayalapati, H.
Discovery of novel putative inhibitors of UDP-GlcNAc 2-epimerase as potent antibacterial agents
ACS Med. Chem. Lett.
4
1142-1147
2013
Bacillus anthracis (Q81K32), Staphylococcus aureus (Q9REV4), Staphylococcus aureus
brenda
Chen, S.C.; Huang, C.H.; Shin Yang, C.; Liu, J.S.; Kuan, S.M.; Chen, Y.
Crystal structures of the archaeal UDP-GlcNAc 2-epimerase from Methanocaldococcus jannaschii reveal a conformational change induced by UDP-GlcNAc
Proteins
82
1519-1526
2014
Methanocaldococcus jannaschii (Q58899), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58899)
brenda
Zhang, L.; Muthana, M.M.; Yu, H.; McArthur, J.B.; Qu, J.; Chen, X.
Characterizing non-hydrolyzing Neisseria meningitidis serogroup A UDP-N-acetylglucosamine (UDP-GlcNAc) 2-epimerase using UDP-N-acetylmannosamine (UDP-ManNAc) and derivatives
Carbohydr. Res.
419
18-28
2016
Neisseria meningitidis serogroup A / serotype 4A (A0A0U1RGY0), Neisseria meningitidis serogroup A /serotype 4A (A0A0U1RGY0), Neisseria meningitidis serogroup A / serotype 4A Z2491 (A0A0U1RGY0), Neisseria meningitidis serogroup A /serotype 4A Z2491 (A0A0U1RGY0)
brenda
Wang, Y.T.; Missiakas, D.; Schneewind, O.
GneZ, a UDP-GlcNAc 2-epimerase, is required for S-layer assembly and vegetative growth of Bacillus anthracis
J. Bacteriol.
196
2969-2978
2014
Bacillus anthracis (Q81K32), Bacillus anthracis (Q81X16), Bacillus anthracis
brenda
Chen, S.; Huang, C.; Shin Yang, C.; Liu, J.; Kuan, S.; Chen, Y.
Crystal structures of the archaeal UDP-GlcNAc 2-epimerase from Methanocaldococcus jannaschii reveal a conformational change induced by UDP-GlcNAc
Proteins
82
1519-1526
2014
Bacillus subtilis (P39131), Bacillus subtilis, Methanocaldococcus jannaschii (Q58899), Methanocaldococcus jannaschii, Bacillus subtilis 168 (P39131)
brenda
Mann, P.A.; Mueller, A.; Wolff, K.A.; Fischmann, T.; Wang, H.; Reed, P.; Hou, Y.; Li, W.; Mueller, C.E.; Xiao, J.; Murgolo, N.; Sher, X.; Mayhood, T.; Sheth, P.R.; Mirza, A.; Labroli, M.; Xiao, L.; McCoy, M.; Gill, C.J.; Pinho, M.G.; Schneider, T.; Roemer, T.
Chemical genetic analysis and functional characterization of staphylococcal wall teichoic acid 2-epimerases reveals unconventional antibiotic drug targets
PLoS Pathog.
12
e1005585
2016
Staphylococcus epidermidis, Staphylococcus aureus (P95709), Staphylococcus aureus (Q9REV4), Staphylococcus aureus, Staphylococcus aureus COL (P95709), Staphylococcus aureus COL (Q9REV4), Staphylococcus epidermidis CLB26329
brenda