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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

Renatured

Renatured on EC 5.1.3.2 - UDP-glucose 4-epimerase

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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
denaturation in presence of 8 M urea. Dilution of the denaturant by sodium phosphate buffer, 20 mM, pH 7.0, containing 1 mM NAD+ recovers the activity to the extent of 80-100%
-
denatured by 8 M urea at pH 7.0 to a state having 15% of residual secondary structure. Dilution of the denaturant by 20 mM potassium phosphate, pH 8.5, leads to functional reconstitution of the enzyme. Reactivation follows a socond-order kinetics
-
dilution of the denaturant urea by buffer at pH 8.5 leads to functional reconstitution of the dimeric holoenzyme. The refolding process is biphasic: after 2 min an equilibrium conformer is formed having 72% of its native secondary structure and by 60 min reactivation becomes complete. The early intermediate has lower energy of activation against thermal denaturation than the reactivated state
-
purified enzyme dimer consists of a mixture of catalytically active subunits designated enzyme-NAD+ and inactive, abortive complexes designated enzyme-NADH-uridine nucleotide, in which the uridine nucleotide may be UDPglucose, UDPgalactose, or UDP. The abortive complexes are transformed into active enzyme-NAD+ by denaturation of the purified enzyme at 4°C in 6 M guanidine hydrochloride buffered at pH 7.0 in the presence of 0.126 mM NAD+ for 3 h, followed by dilution of guanidine hydrochloride to 0.18 M and of NAD+ to 0.076 mM for 2 h. The renatured enzyme is fully active and contains negligible amounts of NADH and uridine nucleotides
-