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Literature summary extracted from

  • Campbell, R.E.; Mosimann, S.C.; Tanner, M.E.; Strynadka, N.C.
    The structure of UDP-N-acetylglucosamine 2-epimerase reveals homology to phosphoglycosyl transferases (2000), Biochemistry, 39, 14993-15001.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.183
-
 Streptococcus pneumoniae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.183 crystal structure of of the selenomethionine-substituted UDP-GlcNAc 2-epimerase enzyme from Escherichia coli is determined at 2.5 resolution by multiple-wavelength anomalous dispersion (MAD) phasing. A structural homology with the enzymes glycogen phosphorylase and T4 phage beta-glucosyltransferase is shown Streptococcus pneumoniae
5.1.3.14 hanging drop vapor diffusion method, selenomethionyl enzyme, X-ray structure at 2.5 A of the enzyme with bound UDP Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.183 additional information selenomethionine-substituted UDP-GlcNAc 2-epimerase is used for crystal structure analysis Streptococcus pneumoniae

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.183 Streptococcus pneumoniae P27828 cf. EC5.1.3.14, bifunctional
-
5.1.3.14 Escherichia coli P27828
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.183
-
 Streptococcus pneumoniae
5.1.3.14
-
 Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.2.1.183 SeMet UDP-GlcNAc 2-epimerase
-
 Streptococcus pneumoniae
3.2.1.183 UDP-N-acetylglucosamine 2-epimerase
-
 Streptococcus pneumoniae