Literature summary for 3.2.1.183 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.

Search for more literature for 3.2.1.183

Cloned(Commentary)

Cloned (Comment)	Organism
-	Streptococcus pneumoniae

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Protein Variants

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

Organism

Organism	UniProt	Comment	Textmining
Streptococcus pneumoniae	P27828	cf. EC5.1.3.14, bifunctional	-

Purification (Commentary)

Purification (Comment)	Organism
-	Streptococcus pneumoniae

Synonyms

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

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)