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Literature summary extracted from

  • Chen, S.; Huang, C.; Shin Yang, C.; Liu, J.; Kuan, S.; Chen, Y.
    Crystal structures of the archaeal UDP-GlcNAc 2-epimerase from Methanocaldococcus jannaschii reveal a conformational change induced by UDP-GlcNAc (2014), Proteins, 82, 1519-1526 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.1.3.14 gene wecB, sequence comparisons, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) Bacillus subtilis
5.1.3.14 gene wecB, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Methanocaldococcus jannaschii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.1.3.14 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
5.1.3.14 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 Methanocaldococcus jannaschii

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.3.14 UDP binding structure, overview Bacillus subtilis
5.1.3.14 UDP binding structure, overview Methanocaldococcus jannaschii

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine Methanocaldococcus jannaschii
-
 UDP-N-acetyl-alpha-D-mannosamine
-
 r
5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine Bacillus subtilis
-
 UDP-N-acetyl-alpha-D-mannosamine
-
 r
5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine Bacillus subtilis 168
-
 UDP-N-acetyl-alpha-D-mannosamine
-
 r

Organism

EC Number Organism UniProt Comment Textmining
5.1.3.14 Bacillus subtilis P39131
-
-
5.1.3.14 Bacillus subtilis 168 P39131
-
-
5.1.3.14 Methanocaldococcus jannaschii Q58899
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.3.14 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, gel filtration, and ultrafiltration Methanocaldococcus jannaschii
5.1.3.14 recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine
-
 Methanocaldococcus jannaschii UDP-N-acetyl-alpha-D-mannosamine
-
 r
5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine
-
 Bacillus subtilis UDP-N-acetyl-alpha-D-mannosamine
-
 r
5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine UDP-GlcNAc binding structure, overview Methanocaldococcus jannaschii UDP-N-acetyl-alpha-D-mannosamine
-
 r
5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine UDP-GlcNAc binding structure, overview Bacillus subtilis UDP-N-acetyl-alpha-D-mannosamine
-
 r
5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine
-
 Bacillus subtilis 168 UDP-N-acetyl-alpha-D-mannosamine
-
 r
5.1.3.14 UDP-N-acetyl-alpha-D-glucosamine UDP-GlcNAc binding structure, overview Bacillus subtilis 168 UDP-N-acetyl-alpha-D-mannosamine
-
 r

Subunits

EC Number Subunits Comment Organism
5.1.3.14 More structural superimposition of closed-form and open-form Mj-epimerase, overview Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
5.1.3.14 Bs-epimerase
-
 Bacillus subtilis
5.1.3.14 Mj-epimerase
-
 Methanocaldococcus jannaschii
5.1.3.14 UDP-GlcNAc 2-epimerase
-
 Methanocaldococcus jannaschii
5.1.3.14 UDP-GlcNAc 2-epimerase
-
 Bacillus subtilis
5.1.3.14 uridine diphosphate N-acetylglucosamine 2-epimerase
-
 Methanocaldococcus jannaschii
5.1.3.14 uridine diphosphate N-acetylglucosamine 2-epimerase
-
 Bacillus subtilis
5.1.3.14 wecB
-
 Methanocaldococcus jannaschii

General Information

EC Number General Information Comment Organism
5.1.3.14 malfunction mutation of this enzyme causes changes in cell morphology and the thermoresistance of the cell wall Methanocaldococcus jannaschii
5.1.3.14 malfunction mutation of this enzyme causes changes in cell morphology and the thermoresistance of the cell wall Bacillus subtilis
5.1.3.14 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
5.1.3.14 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
5.1.3.14 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
5.1.3.14 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