BRENDA - Enzyme Database
show all sequences of 5.1.3.14

Crystal structures of the archaeal UDP-GlcNAc 2-epimerase from Methanocaldococcus jannaschii reveal a conformational change induced by UDP-GlcNAc

Chen, S.; Huang, C.; Shin Yang, C.; Liu, J.; Kuan, S.; Chen, Y.; Proteins 82, 1519-1526 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene wecB, sequence comparisons, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Bacillus subtilis
gene wecB, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
Methanocaldococcus jannaschii
Crystallization (Commentary)
Crystallization
Organism
UDP-GlcNAc 2-epimerase in complex with UDPGlcNAc and UDP, X-ray diffraction structure determination and analysis at 1.69 A resolution, molecular replacement using enzyme structure, PDB ID 3BEO, as search model
Bacillus subtilis
UDP-GlcNAc 2-epimerase in open and closed conformations, and UDP-GlcNAc 2-epimerase in complex with UDPGlcNAc and UDP, sitting drop vapor diffusion method, mixing of 0.001 ml of 5 mg/ml protein in 50 mM Tris-HCl, pH 8.0, 100 mM NaCl, 5% glycerol, and 2 mM tris(2-carboxyethyl)phosphine, with 0.001 ml of reservoir solution containing 40 mM Tris-propane, 60 mM citrate, pH 4.1, and 16% PEG3350, and equilibration against 0.3 ml of reservoir solution at 20C for 1 week, X-ray diffraction structure determination and analysis at 1.42-2.85 A resolution
Methanocaldococcus jannaschii
Inhibitors
Inhibitors
Commentary
Organism
Structure
UDP
binding structure, overview
Bacillus subtilis
UDP
binding structure, overview
Methanocaldococcus jannaschii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
UDP-N-acetyl-alpha-D-glucosamine
Methanocaldococcus jannaschii
-
UDP-N-acetyl-alpha-D-mannosamine
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
Bacillus subtilis
-
UDP-N-acetyl-alpha-D-mannosamine
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
Bacillus subtilis 168
-
UDP-N-acetyl-alpha-D-mannosamine
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus subtilis
P39131
-
-
Bacillus subtilis 168
P39131
-
-
Methanocaldococcus jannaschii
Q58899
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, gel filtration, and ultrafiltration
Methanocaldococcus jannaschii
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)
Bacillus subtilis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
UDP-N-acetyl-alpha-D-glucosamine
-
749249
Methanocaldococcus jannaschii
UDP-N-acetyl-alpha-D-mannosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
-
749249
Bacillus subtilis
UDP-N-acetyl-alpha-D-mannosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-GlcNAc binding structure, overview
749249
Methanocaldococcus jannaschii
UDP-N-acetyl-alpha-D-mannosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-GlcNAc binding structure, overview
749249
Bacillus subtilis
UDP-N-acetyl-alpha-D-mannosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
-
749249
Bacillus subtilis 168
UDP-N-acetyl-alpha-D-mannosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-GlcNAc binding structure, overview
749249
Bacillus subtilis 168
UDP-N-acetyl-alpha-D-mannosamine
-
-
-
r
Subunits
Subunits
Commentary
Organism
More
structural superimposition of closed-form and open-form Mj-epimerase, overview
Methanocaldococcus jannaschii
Cloned(Commentary) (protein specific)
Commentary
Organism
gene wecB, sequence comparisons, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Bacillus subtilis
gene wecB, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
Methanocaldococcus jannaschii
Crystallization (Commentary) (protein specific)
Crystallization
Organism
UDP-GlcNAc 2-epimerase in complex with UDPGlcNAc and UDP, X-ray diffraction structure determination and analysis at 1.69 A resolution, molecular replacement using enzyme structure, PDB ID 3BEO, as search model
Bacillus subtilis
UDP-GlcNAc 2-epimerase in open and closed conformations, and UDP-GlcNAc 2-epimerase in complex with UDPGlcNAc and UDP, sitting drop vapor diffusion method, mixing of 0.001 ml of 5 mg/ml protein in 50 mM Tris-HCl, pH 8.0, 100 mM NaCl, 5% glycerol, and 2 mM tris(2-carboxyethyl)phosphine, with 0.001 ml of reservoir solution containing 40 mM Tris-propane, 60 mM citrate, pH 4.1, and 16% PEG3350, and equilibration against 0.3 ml of reservoir solution at 20C for 1 week, X-ray diffraction structure determination and analysis at 1.42-2.85 A resolution
Methanocaldococcus jannaschii
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
UDP
binding structure, overview
Bacillus subtilis
UDP
binding structure, overview
Methanocaldococcus jannaschii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
UDP-N-acetyl-alpha-D-glucosamine
Methanocaldococcus jannaschii
-
UDP-N-acetyl-alpha-D-mannosamine
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
Bacillus subtilis
-
UDP-N-acetyl-alpha-D-mannosamine
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
Bacillus subtilis 168
-
UDP-N-acetyl-alpha-D-mannosamine
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, gel filtration, and ultrafiltration
Methanocaldococcus jannaschii
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)
Bacillus subtilis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
UDP-N-acetyl-alpha-D-glucosamine
-
749249
Methanocaldococcus jannaschii
UDP-N-acetyl-alpha-D-mannosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
-
749249
Bacillus subtilis
UDP-N-acetyl-alpha-D-mannosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-GlcNAc binding structure, overview
749249
Methanocaldococcus jannaschii
UDP-N-acetyl-alpha-D-mannosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-GlcNAc binding structure, overview
749249
Bacillus subtilis
UDP-N-acetyl-alpha-D-mannosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
-
749249
Bacillus subtilis 168
UDP-N-acetyl-alpha-D-mannosamine
-
-
-
r
UDP-N-acetyl-alpha-D-glucosamine
UDP-GlcNAc binding structure, overview
749249
Bacillus subtilis 168
UDP-N-acetyl-alpha-D-mannosamine
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
More
structural superimposition of closed-form and open-form Mj-epimerase, overview
Methanocaldococcus jannaschii
General Information
General Information
Commentary
Organism
malfunction
mutation of this enzyme causes changes in cell morphology and the thermoresistance of the cell wall
Bacillus subtilis
malfunction
mutation of this enzyme causes changes in cell morphology and the thermoresistance of the cell wall
Methanocaldococcus jannaschii
additional information
comparison of the crystal structures of Methanocaldococcus jannaschii in open and closed conformations and of Bacillus subtilis. Homologous enzyme structure comparisons, overview
Bacillus subtilis
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
Methanocaldococcus jannaschii
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
Bacillus subtilis
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
Methanocaldococcus jannaschii
General Information (protein specific)
General Information
Commentary
Organism
malfunction
mutation of this enzyme causes changes in cell morphology and the thermoresistance of the cell wall
Bacillus subtilis
malfunction
mutation of this enzyme causes changes in cell morphology and the thermoresistance of the cell wall
Methanocaldococcus jannaschii
additional information
comparison of the crystal structures of Methanocaldococcus jannaschii in open and closed conformations and of Bacillus subtilis. Homologous enzyme structure comparisons, overview
Bacillus subtilis
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
Methanocaldococcus jannaschii
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
Bacillus subtilis
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
Methanocaldococcus jannaschii
Other publictions for EC 5.1.3.14
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
747462
Zhang
Characterizing non-hydrolyzin ...
Neisseria meningitidis serogroup A / serotype 4A, Neisseria meningitidis serogroup A / serotype 4A Z2491
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2
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1
1
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2
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2
2
728782
Chen
Crystal structures of the arch ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
Proteins
82
1519-1526
2014
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1
1
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1
1
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748089
Wang
GneZ, a UDP-GlcNAc 2-epimeras ...
Bacillus anthracis
J. Bacteriol.
196
2969-2978
2014
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1
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1
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6
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2
4
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749249
Chen
Crystal structures of the arc ...
Bacillus subtilis 168, Bacillus subtilis, Methanocaldococcus jannaschii
Proteins
82
1519-1526
2014
-
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2
2
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2
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7
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6
1
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6
6
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726555
Xu
Discovery of novel putative in ...
Bacillus anthracis, Staphylococcus aureus
ACS Med. Chem. Lett.
4
1142-1147
2013
-
2
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48
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2
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4
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4
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2
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48
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4
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2
2
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716189
Moeller
Efficient metabolic oligosacch ...
Homo sapiens
Mol. Biosyst.
7
2245-2251
2011
-
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1
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2
2
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703285
Voermans
Clinical features, lectin stai ...
Homo sapiens
Clin. Neuropathol.
29
71-77
2010
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2
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1
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2
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2
2
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703865
Saechao
Novel GNE mutations in heredit ...
Homo sapiens
Genet. Test. Mol. Biomarkers
14
157-162
2010
-
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1
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15
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15
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2
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2
2
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703905
Weidemann
Lessons from GNE-deficient emb ...
Mus musculus
Glycobiology
20
107-117
2010
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1
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1
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1
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1
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3
3
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703912
Kurochkina
Molecular modeling of the bifu ...
Homo sapiens
Glycobiology
20
322-337
2010
-
-
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36
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1
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1
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2
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692536
Reinke
Biochemical characterization o ...
Homo sapiens, Mus musculus
Glycoconj. J.
26
415-422
2009
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2
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702507
Reinke
Regulation and pathophysiologi ...
Homo sapiens, Mus musculus, Rattus norvegicus
Biol. Chem.
390
591-599
2009
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3
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4
4
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689622
Castilho
Construction of a functional C ...
Mus musculus
Plant Physiol.
147
331-339
2008
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1
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692076
Velloso
-
A structural basis for the all ...
Bacillus anthracis
EMBO Rep.
9
1251
2008
1
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1
5
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6
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6
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692855
Namboori
Acetamido sugar biosynthesis i ...
Methanococcus maripaludis
J. Bacteriol.
190
2987-2996
2008
1
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1
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2
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3
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1
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Identification of N-acetylhexo ...
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Changes in sialic acid metabol ...
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Harrington
Biosynthesis of wall teichoic ...
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Kawamura
Biosynthesis of UDP-N-acetyl-D ...
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Van Rinsum
Subcellular localization and t ...
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Corfield
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The metabolism of sialic acids ...
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Corfield
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Changes in the activity of the ...
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2268
Kawamura
UDP-N-acetyl-D-glucosamine 2'- ...
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2267
Kikuchi
UDP-N-acetylglucosamine 2'-epi ...
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2265
Kawamura
Enzymatic synthesis of uridine ...
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2266
Okubo
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Glucosamine-6-P synthetase and ...
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2264
Kawamura
Enzymatic formation of uridine ...
Bacillus cereus, Bacillus megaterium, Bacillus subtilis, Escherichia coli, Micrococcus luteus, Staphylococcus aureus
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Salo
The incorporation of tritium f ...
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Biochim. Biophys. Acta
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625-628
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2262
Kawamura
Biosynthesis of uridine diphos ...
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Kikuchi
Purification and properties of ...
Rattus norvegicus
Biochim. Biophys. Acta
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1973
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2259
Sommar
Uridine diphosphate N-acetyl-D ...
Rattus norvegicus
Biochim. Biophys. Acta
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581-589
1972
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Sommar
Uridine diphosphate N-acetyl-D ...
Rattus norvegicus
Biochim. Biophys. Acta
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590-595
1972
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Salo
Studies on the mechanism of ac ...
Rattus norvegicus
Biochemistry
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Spivak
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UDP-N-acetyl-D-glucosamine 2'- ...
Rattus norvegicus
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612-615
1966
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