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Information on EC 5.1.3.14 - UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing) and Organism(s) Rattus norvegicus and UniProt Accession O35826
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5.1.3.14 UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing)IUBMB Comments
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).
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Word Map
- 5.1.3.14
-
sialic
- myopathy
- hereditary
-
rimmed
-
sialylation
- vacuoles
-
n-acetylneuraminic
-
quadriceps
- sialuria
- glycoconjugates
-
hyposialylation
- udp-n-acetylmannosamine
-
nonaka
- neu5ac
-
inclusion-body
- drug development
- cmp-neu5ac
-
cmp-n-acetylneuraminic
-
cmp-sialic
- medicine
- synthesis
- biotechnology
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
udp-n-acetylglucosamine 2-epimerase/n-acetylmannosamine kinase, udp-glcnac 2-epimerase, udp-n-acetylglucosamine 2-epimerase, udp-n-acetylglucosamine-2-epimerase/n-acetylmannosamine kinase, udp-glcnac 2-epimerase/mannac kinase, gne/mnk, cap5p, udp-glcnac-2-epimerase, udp-n-acetylglucosamine-2-epimerase, nmsaca, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Epimerase, uridine diphosphoacetylglucosamine 2-
-
-
-
-
UDP-GlcNAc 2'-epimerase
-
-
-
-
UDP-GlcNAc-2-epimerase
-
-
-
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UDP-N-acetylglucosamine 2'-epimerase
-
-
-
-
UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
Uridine diphosphate-N-acetylglucosamine-2'-epimerase
-
-
-
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Uridine diphospho-N-acetylglucosamine 2'-epimerase
-
-
-
-
Uridine diphosphoacetylglucosamine 2'-epimerase
-
-
-
-
additional information
UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
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bifunctional
UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
-
bifunctional enzyme
additional information
-
bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/ManNAc kinase
additional information
-
bifunctional enzyme UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-mannosamine
UDP-N-acetyl-D-mannosamine is not an intermediate
-
UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-mannosamine
products: UDP + N-acetyl-D-mannosamine
-
UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-mannosamine
ordered mechanism, where UDP is the first product released followed by irreversible formation of N-acetyl-mannosamine. A two step mechanism is proposed which involves the elimination of UDP from UDP-N-acetylglucosamine to give a 2-acetamidoglucal intermediate which is subsequently converted to N-acetylmannosamine
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
epimerization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -
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
9037-71-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-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
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-D-mannosamine
-
key enzyme of sialic acid biosynthesis
-
-
?
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
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2',3'-dialdehydro-ADP
-
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-alpha-D-N-acetylglucosamine
-
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
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
-
-
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
-
-
uridine 5'-[(Z)-3-acetamido-2,6-anhydro-1,3-dideoxy-D-gluco-hept-1-enitol-1-yl phosphono] phosphate
-
-
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.08
UDP-N-acetyl-D-glucosamine
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UDP-N-acetyl-D-glucosamine, liver enzyme of tumor-bearing animals
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8.6
-
6.5: about 30% of maximal activity, 8.6: about 65% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
enzyme is detected only in sialoglycoprotein-secreting tissues
-
enzyme activity is significantly elevated at 8 h after intradermal injection of carageenan or urate crystals, falling to normal levels by day 3
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enzyme activity is 18% of the activity found in normal livers
-
enzyme is detected only in sialoglycoprotein-secreting tissues
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enzyme is detected only in sialoglycoprotein-secreting tissues
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colonic mucosa: normal mucosa, non-malignant mucosa in azomethane treated animals, low activity in azomethane-induced tumor tissue
-
activity in colonic tissue is 25-50times lower than in liver
-
enzyme activity is significantly elevated at 8 h after intradermal injection of carrageenan or urate crystals, falling to normal levels by day 3
-
enzyme activity is low at birth, increases to a maximum value on day 15, and falls gradually until day 30, thereafter it increases up to the 60th day
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
additional information
-
comparison of the GNE primary structures reveals a high sequence similarity between human and rodent GNE, indicating high evolutionary conservation
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
H155A
H157A
R420M
-
enzyme with mutation in the putative kinase active site shows drastic loss in their kinase activity but retains their epimerase activity
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the purified enzyme is 80% pure, no further purification because it is unstable to freezing and has limited stability upon storage at 4°C
-
UDP and UDP-N-acetylglucosamine protect the enzyme from inactivation by aging
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10°C, overnight, in a saturated (NH4)2SO4 solution, approximately 20% loss of activity
-
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
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme expressed in Escherichia coli and enzyme expressed in insect cells
-
recombinant enzyme expressed in Spodoptera frugiperda cells using a baculovirus expression system
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
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
-
high level overexpression of the active enzyme is established by using the baculovirus/Sf9 system
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
production of erythropoietin (EPO) in Chinese Hamster Ovary (CHO) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Spivak, C.T.; Roseman, S.
UDP-N-acetyl-D-glucosamine 2'-epimerase
Methods Enzymol.
9
612-615
1966
Rattus norvegicus
-
Salo, W.L.; Fletcher, H.G.
Studies on the mechanism of action of uridine diphosphate N-acetylglucosamine 2-epimerase
Biochemistry
9
882-885
1970
Rattus norvegicus
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
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
590-595
1972
Rattus norvegicus
Kikuchi, K.; Tsuiki, S.
Purification and properties of UDP-N-acetylglucosamine 2'-epimerase from rat liver
Biochim. Biophys. Acta
327
193-206
1973
Rattus norvegicus
Okubo, H.; Shibata, K.; Ishibashi, H.; Kudo, J.; Miyanaga, O.; Nagano, M.
Glucosamine-6-P synthetase and UDP-GlcNAc 2'-epimerase activities in tumor-bearing animals
Jpn. J. Clin. Chem.
8
99-103
1979
Rattus norvegicus
-
Kikuchi, K.; Tsuiki, S.
UDP-N-acetylglucosamine 2'-epimerase of rat hepatoma and its comparison with the enzyme of rat liver
Tohoku J. Exp. Med.
131
209-214
1980
Mus musculus, Rattus norvegicus
Van Rinsum, J.; van Dijk, W.; Hooghwinkel, G.J.M.; Ferwerda, W.
Subcellular localization and tissue distribution of sialic acid precursor-forming enzymes
Biochem. J.
210
21-28
1983
Rattus norvegicus
Corfield, A.P.; Clamp, J.R.; Wagner, S.A.
The metabolism of sialic acids in isolated rat colonic mucosal cells
Biochem. Soc. Trans.
11
767-768
1983
Rattus norvegicus
-
Zeitler, R.; Banzer, J.P.; Bauer, C.; Reutter, W.
Inhibition of the biosynthesis of N-acetylneuraminic acid by metal ions and selenium in vitro
Biometals
5
103-109
1992
Rattus norvegicus
Gal, B.; Ruano, M.J.; Puente, R.; Garcia-Pardo, L.A.; Rueda, R.; Gil, A.; Hueso, P.
Developmental changes in UDP-N-acetylglucosamine 2-epimerase activity in rat and guinea-pig liver
Comp. Biochem. Physiol. B
118
13-15
1997
Cavia porcellus, Rattus norvegicus
Stsche, R.; Hinderlich, S.; Weise, C.; Effertz, K.; Lucka, L.; Moormann, P.; Reutter, W.
A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. Molecular cloning and functional expression of UDP-N-acetyl-glucosamine 2-epimerase/N-acetylmannosamine kinase
J. Biol. Chem.
272
24319-24324
1997
Rattus norvegicus (O35826)
Hinderlich, S.; Stsche, R.; Zeitler, R.; Reutter, W.
A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. Purification and characterization of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
J. Biol. Chem.
272
24313-24318
1997
Rattus norvegicus
Corfield, A.P.; Hutton, C.W.; Clamp, J.R.; Dieppe, P.A.
Changes in sialic acid metabolism occur in colon and liver during the acute-phase response
Biochem. Soc. Trans.
14
628-629
1986
Rattus norvegicus
-
Corfield, A.P.; Rainey, J.B.; Clamp, J.R.; Wagner, S.A.
Changes in the activity of the enzymes involved in sialic acid metabolism in isolated rat colonic mucosal cells on administration of azoxymethane
Biochem. Soc. Trans.
11
766-767
1983
Rattus norvegicus
-
Effertz, K.; Hinderlich, S.; Reutter, W.
Selective loss of either the epimerase or kinase activity of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase due to site-directed mutagenesis based on sequence alignments
J. Biol. Chem.
274
28771-28778
1999
Rattus norvegicus
Blume, A.; Chen, H.; Reutter, W.; Schmidt, R.R.; Hinderlich, S.
2',3'-Dialdehydo-UDP-N-acetylglucosamine inhibits UDP-N-acetylglucosamine 2-epimerase, the key enzyme of sialic acid biosynthesis
FEBS Lett.
521
127-132
2002
Rattus norvegicus
Chou, W.K.; Hinderlich, S.; Reutter, W.; Tanner, M.E.
Sialic acid biosynthesis: stereochemistry and mechanism of the reaction catalyzed by the mammalian UDP-N-acetylglucosamine 2-epimerase
J. Am. Chem. Soc.
125
2455-2461
2003
Rattus norvegicus
Stolz, F.; Reiner, M.; Blume, A.; Reutter, W.; Schmidt, R.R.
Novel UDP-glycal derivatives as transition state analogue inhibitors of UDP-GlcNAc 2-epimerase
J. Org. Chem.
69
665-679
2004
Rattus norvegicus
Blume, A.; Weidemann, W.; Stelzl, U.; Wanker, E.E.; Lucka, L.; Donner, P.; Reutter, W.; Horstkorte, R.; Hinderlich, S.
Domain-specific characteristics of the bifunctional key enzyme of sialic acid biosynthesis, UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
Biochem. J.
384
599-607
2004
Rattus norvegicus
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
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
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
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
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