UDP-N-acetylglucosamine 2-epimerase (hydrolysing)

UDP-N-acetylglucosamine 2-epimerase (hydrolysing)
Identifiers
EC number 3.2.1.183
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

UDP-N-acetylglucosamine 2-epimerase (hydrolysing) (EC 3.2.1.183, UDP-N-acetylglucosamine 2-epimerase, GNE (gene), siaA (gene), neuC (gene)) is an enzyme with systematic name UDP-N-acetyl-alpha-D-glucosamine hydrolase (2-epimerising).[1][2][3][4] This enzyme catalyses the following chemical reaction

UDP-N-acetyl-alpha-D-glucosamine + H2O N-acetyl-D-mannosamine + UDP

The enzyme is found in mammalian liver, as well as in some pathogenic bacteria including Neisseria meningitidis and Staphylococcus aureus.

References

  1. ↑ Stäsche R, Hinderlich S, Weise C, Effertz K, Lucka L, Moormann P, Reutter W (September 1997). "A bifunctional enzyme catalyzes the first two steps in N-acetylneuraminic acid biosynthesis of rat liver. Molecular cloning and functional expression of UDP-N-acetyl-glucosamine 2-epimerase/N-acetylmannosamine kinase". The Journal of Biological Chemistry. 272 (39): 24319–24. doi:10.1074/jbc.272.39.24319. PMID 9305888.
  2. ↑ Chou WK, Hinderlich S, Reutter W, Tanner ME (March 2003). "Sialic acid biosynthesis: stereochemistry and mechanism of the reaction catalyzed by the mammalian UDP-N-acetylglucosamine 2-epimerase". Journal of the American Chemical Society. 125 (9): 2455–61. doi:10.1021/ja021309g. PMID 12603133.
  3. ↑ Blume A, Ghaderi D, Liebich V, Hinderlich S, Donner P, Reutter W, Lucka L (June 2004). "UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, functionally expressed in and purified from Escherichia coli, yeast, and insect cells". Protein Expression and Purification. 35 (2): 387–96. doi:10.1016/j.pep.2004.02.013. PMID 15135418.
  4. ↑ Murkin AS, Chou WK, Wakarchuk WW, Tanner ME (November 2004). "Identification and mechanism of a bacterial hydrolyzing UDP-N-acetylglucosamine 2-epimerase". Biochemistry. 43 (44): 14290–8. doi:10.1021/bi048606d. PMID 15518580.
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