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5.1.3.2: UDP-glucose 4-epimerase

This is an abbreviated version!
For detailed information about UDP-glucose 4-epimerase, go to the full flat file.

Word Map on EC 5.1.3.2

Reaction

UDP-alpha-D-glucose
=
UDP-alpha-D-galactose

Synonyms

4-Epimerase, 6xHis-rGalE, ABD1_580, An14g03820, AtUGE1, AtUGE2, AtUGE3, AtUGE4, AtUGE5, CaGAL10, CapD, epimerase Ab-WbjB, Epimerase, uridine diphosphoglucose, fnlA, GAL10, Gal10p, Galactowaldenase, GalE, galE-1, galE-2, galE1, GalESp1, GalESp2, GNE, GNE2, H3634, HvUGE1, HvUGE2, HvUGE3, MdUGE1, More, OsUGE-1, OsUGE1, PsUGE1, Rdh1, rGalE, Rv3634c, TbGalE, TM0509, TMGalE, UDP-D-galactose 4-epimerase, UDP-D-glucose/UDP-D-galactose 4-epimerase, UDP-Gal 4-epimerase, UDP-Gal/Glc 4-epimerase, UDP-galactose 4'-epimerase, UDP-galactose 4-epimerase, UDP-galactose-4'-epimerase, UDP-galactose-4-epimerase, UDP-Glc 4-epimerase, UDP-Glc(NAc) 4-epimerase, UDP-GlcNAc 4-epimerase, UDP-GlcNAc/Glc 4-epimerase, UDP-glucose 4'-epimerase, UDP-glucose 4-epimerase, UDP-glucose 4-epimerase 1, UDP-glucose 4-epimerase 4, UDP-glucose epimerase, UDP-glucose-4-epimerase, UDP-glucose/-galactose 4-epimerase, UDP-hexose 4-epimerase, UDP-N-acetyl-glucosamine 4,6-dehydratase, UDP-sugar 4-epimerase, UDP-Xyl 4-epimerase, UDP-xylose 4-epimerase, UDPG-4-epimerase, UDPgalactose 4-epimerase, UGE, UGE-1, UGE1, UGE1:GUS, Uge1p, UGE2, UGE3, UGE3:GUS, UGE4, UGE5, UgeA, Uridine diphosphate galactose 4-epimerase, Uridine diphosphate glucose 4-epimerase, uridine diphosphate-galactose-4'-epimerase, Uridine diphospho-galactose-4-epimerase, Uridine diphosphogalactose-4-epimerase, Uridine diphosphoglucose 4-epimerase, Uridine diphosphoglucose epimerase, uridine-diphospho-glucose 4-epimerase, WbjB

ECTree

     5 Isomerases
         5.1 Racemases and epimerases
             5.1.3 Acting on carbohydrates and derivatives
                5.1.3.2 UDP-glucose 4-epimerase

Crystallization

Crystallization on EC 5.1.3.2 - UDP-glucose 4-epimerase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme Ab-WbjB, hanging drop vapour diffusion method, in an 1:1 ratio mixture from 0.2 M NaCl, 0.1 M HEPES, pH 5.6, and 25% v/v PEG 3350, X-ray diffraction structure determination and analysis at 2.64-2.70 A, method optimization, overview, molecular replacement using the structure of Helicobacter pylori FlaA1 (PDB ID 2gn4) as template
purified recombinant enzyme in complex with UDP-galactose using the microbatch method, 15 mg/ml protein in 25 mM Tris, pH 8, is used with crystallization solution containing 20% w/v PEG 3350, 0.1 M Bis-Tris propane, pH 7.5, and 0.2 M sodium fluoride, 2 weeks, X-ray diffraction structure determination and analysis at 2.4 A resolution
purified recombinant His-tagged enzyme, microbatch method, 4°C, mixing of equal volumes of protein and precipitant solution, the latter containing 20% w/v PEG 3350, 0.1 M Bis-Tris propane pH 7.5, 0.2 M sodium fluoride, cryoprotection with 25% glycerol, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular replacement
crystal structure of the oxidized and reduced forms of UDP-galactose 4-epimerase
crystal structure of the ternary complex of UDP-galactose 4-epimerase with NADH and UDP-phenol
-
crystallization of the epimerase/UDP-GLcNAc/NADH abortive complex
suitable crystallization conditions are both at room temperature and at 4°C using sparse matrix screen and the hanging drop method of vapor diffusion. The best crystals are observed growing from polyethylene glycol 8000 and potassium chloride and in the presence of 2 mM NAD+. Typical large crystals are ontained from 18-20% polyethylene glycol 8000, 100 mM Hepes, pH 7.5, and 250 mM KCl at room temperature, crystallization of a epimerase/NADH/UDP-glucose ternary complex
-
sitting drop vapor diffusion method, using 29% (v/v) 2-ethoxyethanol and 0.1 M cacodylate buffer (pH 6.6), at 20°C
hanging drop vapor diffusion methodthree-dimensional structure of gal10p in complex with NAD+, UDP-glucose, and beta-D-galactose is determined to 1.85 A resolution. Space group I222 with unit cell dimensions of a = 120.9 A, b = 125.2 A and c = 142.3 A. The asymmetric unit contains one monomer
-
hanging drop vapor diffusion method, crystal structure of the enzyme (TMGalE) and the enzyme bound to UDP-glucose is determined at resolutions of 1.9 A and 2.0 A, respectively
purified recombinant unbound enzyme TMGalE, and TMGalE bound to UDP-Glc, X-ray diffraction structure determination and analysis at 1.9-2.0 A resolution
hanging drop method
-