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5.1.3.14: UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing)

This is an abbreviated version!
For detailed information about UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing), go to the full flat file.

Word Map on EC 5.1.3.14

Reaction

UDP-N-acetyl-alpha-D-glucosamine
=
UDP-N-acetyl-alpha-D-mannosamine

Synonyms

bas5048, bas5117, Bs-epimerase, Cap5P, Epimerase, uridine diphosphoacetylglucosamine 2-, GNE, GNE/MNK, GNE1, GNE2, GneY, GneZ, His-rGNE, Mj-epimerase, MnaA, More, NeuC protein, NmSacA, non-hydrolyzing Neisseria meningitidis serogroup A UDP-GlcNAc 2-epimerase, non-hydrolyzing Neisseria meningitidis serogroup A UDP-N-acetylglucosamine 2-epimerase, non-hydrolyzing UDP-GlcNAc 2-epimerase, non-hydrolyzing UDP-N-acetylglucosamine 2-epimerase, non-hydrolyzing uridine 5'-diphosphate-N-acetylglucosamine 2-epimerase, SacA, teichoic acid 2-epimerase, UDP-GlcNAc 2'-epimerase, UDP-GlcNAc 2-epimerase, UDP-GlcNAc 2-epimerase/ManAc kinase, UDP-GlcNAc 2-epimerase/ManNAc kinase, UDP-GlcNAc 2-epimerase/ManNAc kinase gene, UDP-GlcNAc-2-epimerase, UDP-GlcNAc:UDP-ManNAc 2-epimerase, UDP-N-acetylglucosamine 2'-epimerase, UDP-N-acetylglucosamine 2-epimerase, UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, UDP-N-acetylglucosamine-2-epimerase, UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase, uridine diphosphate N-acetylglucosamine 2-epimerase, Uridine diphosphate-N-acetylglucosamine-2'-epimerase, Uridine diphospho-N-acetylglucosamine 2'-epimerase, Uridine diphosphoacetylglucosamine 2'-epimerase, wecB, WTA 2-epimerase

ECTree

     5 Isomerases
         5.1 Racemases and epimerases
             5.1.3 Acting on carbohydrates and derivatives
                5.1.3.14 UDP-N-acetylglucosamine 2-epimerase (non-hydrolysing)

Crystallization

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

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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
-
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
vapor diffusion method
-
hanging drop vapor diffusion method, selenomethionyl enzyme, X-ray structure at 2.5 A of the enzyme with bound UDP
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
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 20°C for 1 week, X-ray diffraction structure determination and analysis at 1.42-2.85 A resolution
purified enzyme MnaA, hanging drop vapor diffusion method, mixing of 31 mg/ml protein solution with crystallization solution containing 0.1 M Tris-HCl, pH 8.0, 0.1 M Na2SO4, 52% PEG 400, 22°C, method optimization, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement using structure PDB ID 1F6D as template