Literature summary for 5.1.3.14 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 .

Cloned(Commentary)

Cloned (Comment)	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 (Comment)	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 20°C for 1 week, X-ray diffraction structure determination and analysis at 1.42-2.85 A resolution	Methanocaldococcus jannaschii

Crystallization (Comment)

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 20°C for 1 week, X-ray diffraction structure determination and analysis at 1.42-2.85 A resolution

Methanocaldococcus jannaschii

Inhibitors

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

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
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	UniProt	Comment	Textmining
Bacillus subtilis	P39131	-	-
Bacillus subtilis 168	P39131	-	-
Methanocaldococcus jannaschii	Q58899	-	-

Purification (Commentary)

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

Subunits

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

Synonyms

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

General Information

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