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Literature summary extracted from

  • Chen, S.C.; Huang, C.H.; Shin Yang, C.; Liu, J.S.; Kuan, S.M.; 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 expression in Escherichia coli Methanocaldococcus jannaschii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.1.3.14 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 Methanocaldococcus jannaschii

Organism

EC Number Organism UniProt Comment Textmining
5.1.3.14 Methanocaldococcus jannaschii Q58899
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5.1.3.14 Methanocaldococcus jannaschii DSM 2661 Q58899
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Synonyms

EC Number Synonyms Comment Organism
5.1.3.14 UDP-GlcNAc 2-epimerase
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 Methanocaldococcus jannaschii

General Information

EC Number General Information Comment Organism
5.1.3.14 metabolism the enzyme catalyzes the interconversion of UDP-N-acetyl-alpha-D-glucosamine to UDP-N-acetyl-alpha-D-mannosamine, which is used in the biosynthesis of cell surface polysaccharides in bacteria Methanocaldococcus jannaschii