Information on EC 5.1.3.14 - UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
5.1.3.14
-
RECOMMENDED NAME
GeneOntology No.
UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-mannosamine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
epimerization
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
-
-
Metabolic pathways
-
-
poly(3-O-beta-D-glucopyranosyl-N-acetylgalactosamine 1-phosphate) wall teichoic acid biosynthesis
-
-
poly(glycerol phosphate) wall teichoic acid biosynthesis
-
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poly(ribitol phosphate) wall teichoic acid biosynthesis I (B. subtilis)
-
-
poly(ribitol phosphate) wall teichoic acid biosynthesis II (S. aureus)
-
-
UDP-N-acetyl-alpha-D-mannosaminouronate biosynthesis
-
-
metabolism of amino sugars and derivatives
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine 2-epimerase
This bacterial enzyme catalyses the reversible interconversion of UDP-GlcNAc and UDP-ManNAc. The latter is used in a variety of bacterial polysaccharide biosyntheses. cf. EC 3.2.1.183, UDP-N-acetylglucosamine 2-epimerase (hydrolysing).
CAS REGISTRY NUMBER
COMMENTARY hide
9037-71-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
K1
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
MC58 group B
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-Acetyl-D-glucosamine
?
show the reaction diagram
-
-
-
-
-
N-Acetyl-D-glucosamine 1-phosphate
?
show the reaction diagram
-
-
-
-
-
UDP-GlcNAc
ManNAc + UDP
show the reaction diagram
UDP-GlcNAc + H2O
ManNAc + UDP
show the reaction diagram
-
biosynthesis of sialic acids
-
-
?
UDP-glucose
?
show the reaction diagram
-
-
-
-
-
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
show the reaction diagram
UDP-N-acetyl-D-glucosamine
?
show the reaction diagram
UDP-N-acetyl-D-glucosamine
UDP + N-acetyl-D-mannosamine
show the reaction diagram
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
show the reaction diagram
UDP-N-acetyl-D-glucosamine + H2O
UDP + N-acetylmannosamine
show the reaction diagram
UDP-N-acetylgalactosamine
?
show the reaction diagram
-
-
-
-
-
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-GlcNAc
ManNAc + UDP
show the reaction diagram
UDP-GlcNAc + H2O
ManNAc + UDP
show the reaction diagram
-
biosynthesis of sialic acids
-
-
?
UDP-N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-mannosamine
show the reaction diagram
UDP-N-acetyl-D-glucosamine
?
show the reaction diagram
UDP-N-acetyl-D-glucosamine
UDP + N-acetyl-D-mannosamine
show the reaction diagram
UDP-N-acetyl-D-glucosamine + H2O
UDP + N-acetylmannosamine
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
increases activity
additional information
-
not stimulated by any metal ion
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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
-
-
CMP-N-acetylneuraminic acid
CMP-Neu5Ac
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
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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
Selenite
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UDPglucose
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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
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KCl
200 mM, twofold stimualtion
UDP-GlcNAc
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allosteric activitation by substrate via direct interactions between UDP and substrate
UDP-N-acetyl-D-glucosamine
-
allosteric activation
UDP-N-acetylglucosamine
additional information
-
enzyme does not contain a tightly bound NAD+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.011 - 20.9
UDP-N-acetyl-D-glucosamine
0.63
UDP-N-acetylglucosamine
-
-
0.22 - 1
UDP-N-acetylmannosamine
additional information
additional information
Hill coefficient of 2.7, positive cooperativity
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.021 - 7.9
UDP-N-acetyl-D-glucosamine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
CMP-N-acetylneuraminic acid
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.9
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enzyme expressed in Sf-900 insect cells and purified
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1
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and a second optimum at pH 7.9
7.5 - 8
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7.5
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assay at
7.9
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and a second optimum at pH 7.1
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.6
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6.5: about 30% of maximal activity, 8.6: about 65% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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HIV-infected. Downregulation of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase in hyposialylated HIV-infected T cells
Manually annotated by BRENDA team
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cell proliferation is directly correlated with GNE-expression and the cellular sialic acid concentration. Growth-related genes are differentially expressed in GNE-deficient embryonic stem cells compared to wild-type embryonic stem cells
Manually annotated by BRENDA team
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skin
Manually annotated by BRENDA team
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enzyme activity is 18% of the activity found in normal livers
Manually annotated by BRENDA team
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human epithel, HEK AD293
Manually annotated by BRENDA team
additional information
-
GNE2 and GNE3 display tissue-specific expression patterns
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Burkholderia vietnamiensis (strain G4 / LMG 22486)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Rickettsia bellii (strain RML369-C)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000
-
2 * 38000, SDS-PAGE
39368
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x * 39368, calculation from nucleotide sequence
42400
2 * 40000, SDS-PAGE, 2 * 42400, calculated, recombinant enzyme
75000
-
6 * 75000, SDS-PAGE
76000
-
gel filtraton
79000
x * 79000, calculation from nucleotide sequence
85000
-
6 * 85000, SDS-PAGE
101000
gel filtration
330000
-
dynamic light-scattering
450000
-
gel filtration
500000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ternary complex between the UDP-GlcNAc 2-epimerase, its substrate UDP-GlcNAc and the reaction intermediate UDP, at 1.7 A resolution. Direct interactions between the substrate and UDP via two hydrogen bonds to the alpha- and beta-phosphates of the adjacent UDP molecule, and between the complex and highly conserved enzyme residues. The binding of UDP-GlcNAc is associated with conformational changes in the active site of the enzyme
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vapor diffusion method
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hanging drop vapor diffusion method, selenomethionyl enzyme, X-ray structure at 2.5 A of the enzyme with bound UDP
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sitting-drop vapor-diffusion method, crystal structures in open and closed conformations. A comparison of these crystal structures shows that upon UDP and UDPGlcNAc binding, the enzyme undergoes conformational changes involving a rigid-body movement of the C-terminal domain
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
DTT protects against inactivation at 4 C
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the purified enzyme is 80% pure, no further purification because it is unstable to freezing and has limited stability upon storage at 4°C
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UDP and UDP-N-acetylglucosamine protect the enzyme from inactivation by aging
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10°C, overnight, in a saturated (NH4)2SO4 solution, approximately 20% loss of activity
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-18°C, stable for several months
-70°C, stable for several months
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2°C, several days, maintains well over 50% of its activity
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4°C, 80-90% loss of activity after 60 h
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4°C, in presence of 0.1 mM UDP and 1 mM DTT, 3 days, 20% loss of activity
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4°C, purified enzyme expressed in insect cells, stable
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4°C, purified enzyme is 80% pure, no further purification because it is unstable to freezing and has limited stability upon storage at 4°C
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
bifunctional enzyme EC 5.1.3.14/EC 2.7.1.60
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enzyme expressed in Escherichia coli and enzyme expressed in insect cells
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recombinant enzyme expressed in Spodoptera frugiperda cells using a baculovirus expression system
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recombinant wild-type and mutant enzymes, His-tagged proteins
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
bifunctional enzyme EC 5.1.3.14/EC 2.7.1.60, expressed in COS7 cells
cloning of the neuC gene into an intein expression vector to facilitate purification
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DNA sequencing of the GNE coding region of 64 symptomatic patients with autosomal recessive hereditary inclusion body myopathy, genotyping-phenotyping of patients from different ethnics, overview
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expression in Arabidopsis thaliana
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expression in Chinese Hamster Ovary (CHO)
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expression in Escherichia coli
expression in Escherichia coli, C-terminal His-tag
expression in insect cells
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expression in Insect Cells and supercompetent InvalphaF' Escherichia coli cells (Invitrogen)
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expression in Sf9 insect cells, wild-type enzyme and mutant enzymes DELTA1-39, DELTA1-234, DELTA1-356, DELTA383-722, DELTA490-722, DELTA597-722, DELTA697-722, DELTA717-722
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expression of M712T mutant enzyme in Sf9 insect cells
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expression of wild-type and mutant enzymes (C13S, H132Q, D176V, D177C, V331A, I472T, G708S, A631V, V572L and A630T) in COS-7 cells
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functional expression in Escherichia coli, Saccharomyces cerevisiae, Pichia pastoris or insect cells. In all cell types, the expressed enzyme displayes both epimerase and kinase activities. In Escherichia coli up to 2 mg protein/l cell culture is expressed in yeast cells only 0.4 mg/ml, in insect cells up to 100 mg/L. In all three cell systems, insoluble protein aggregates are also observed. Expression and purification of the UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase in Sf-900 cells can yield the miligram amount of protein required for structural characterization of the enzyme. The easier expression in Escherichia coli and yeast provides sufficient quantities for enzymatic and kinetic characterization
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high level overexpression of the active enzyme is established by using the baculovirus/Sf9 system
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overexpression in Escherichia coli
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overexpression in Escherichia coli BL21(DE3), wild-type enzyme and mutant enzymes D100N, E122Q and D131N
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proteome expression analysis in wild-type and GNE-deficient embryonic stem cells, overview. GNE overexpression in HEK cells
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splice variant hGNE2, expression in insect and mammalian cells. Splice variant hGNE3, expression in Escherichia coli
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splice variants mGNE1, mGNE2, mGNE3
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wild-type and mutant enzymes expressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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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
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a naturally occuring missense mutation in exon 3 of the GNE gene of a patient with hereditary inclusion body myopathy
R8X
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a naturally occuring nonsense mutation in exon 2 of the GNE gene of a patient with hereditary inclusion body myopathy
S615X
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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
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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
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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
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a naturally occuring nonsense mutation in exon 3 of the GNE gene of a patient with hereditary inclusion body myopathy
Y675H
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a naturally occuring missense mutation in exon 12 of the GNE gene of a patient with hereditary inclusion body myopathy
D100N
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no conversion of UDP-N-acetyl-D-glucosamine to UDP + N-acetyl-D-mannosamine
D131N
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no conversion of UDP-N-acetyl-D-glucosamine to UDP + N-acetyl-D-mannosamine, acetamidoglucal is released from the active site during catalysis
E122Q
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no conversion of UDP-N-acetyl-D-glucosamine to UDP + N-acetyl-D-mannosamine, acetamidoglucal is released from the active site during catalysis
D100N
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no conversion of UDP-N-acetyl-D-glucosamine to UDP + N-acetyl-D-mannosamine
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D131N
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no conversion of UDP-N-acetyl-D-glucosamine to UDP + N-acetyl-D-mannosamine, acetamidoglucal is released from the active site during catalysis
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E122Q
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no conversion of UDP-N-acetyl-D-glucosamine to UDP + N-acetyl-D-mannosamine, acetamidoglucal is released from the active site during catalysis
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D413K
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enzyme with mutation in the putative kinase active site shows drastic loss in their kinase activity but retains their epimerase activity
D413N
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enzyme with mutation in the putative kinase active site shows drastic loss in their kinase activity but retains their epimerase activity
DELTA1-234
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mutant enzyme shows no N-epimerase activity
DELTA1-356
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mutant enzyme shows no N-epimerase activity
DELTA1-39
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mutant enzyme shows no N-epimerase activity
DELTA383-722
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epimerase activity is 2% of wild-type enzyme
DELTA490-722
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epimerase activity is 15% of wild-type enzyme
DELTA597-722
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epimerase activity is 2% of wild-type enzyme
DELTA697-722
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epimerase activity is about 70% of wild-type enzyme
DELTA717-722
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epimerase activity is about 95% of wild-type enzyme
H110A
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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
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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
H155A
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mutant enzyme forms mainly trimeric enzyme with small amounts of hexamer; mutant enzyme shows a drastic loss of epimerase activity, loss of epimerase activity can largely by attributed to incorrect protein folding
H157A
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mutant enzyme forms mainly trimeric enzyme with small amounts of hexamer; mutant enzyme shows a drastic loss of epimerase activity, loss of epimerase activity can largely by attributed to incorrect protein folding
H45A
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mutant enzyme shows a drastic loss of epimerase activity
R420M
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enzyme with mutation in the putative kinase active site shows drastic loss in their kinase activity but retains their epimerase activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
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production of erythropoietin (EPO) in Chinese Hamster Ovary (CHO) cells
drug development
medicine
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UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase interacts with the non-muscle form of alpha-actinin, alpha-actinin-1, in mature skeletal muscle cells. No significant difference in the binding of alpha-actinin-1 with either wild-type or mutant enzyme, and therefore no conclusions wether and how the interaction is relevant to the muscle-restricted pathology of hereditary inclusion body myopathy
synthesis
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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
Show AA Sequence (3894 entries)
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