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 \rightleftharpoons 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. Stasche, R., Hinderlich, S., Weise, C., Effertz, K., Lucka, L., Moormann, P. and Reutter, W. (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". J. Biol. Chem. 272: 24319–24324. doi:10.1074/jbc.272.39.24319. PMID 9305888.
  2. Chou, W.K., Hinderlich, S., Reutter, W. and Tanner, M.E. (2003). "Sialic acid biosynthesis: stereochemistry and mechanism of the reaction catalyzed by the mammalian UDP-N-acetylglucosamine 2-epimerase". J. Am. Chem. Soc. 125 (9): 2455–2461. doi:10.1021/ja021309g. PMID 12603133.
  3. Blume, A., Ghaderi, D., Liebich, V., Hinderlich, S., Donner, P., Reutter, W. and Lucka, L. (2004). "UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, functionally expressed in and purified from Escherichia coli, yeast, and insect cells". Protein Expr. Purif. 35 (2): 387–396. doi:10.1016/j.pep.2004.02.013. PMID 15135418.
  4. Murkin, A.S., Chou, W.K., Wakarchuk, W.W. and Tanner, M.E. (2004). "Identification and mechanism of a bacterial hydrolyzing UDP-N-acetylglucosamine 2-epimerase". Biochemistry 43 (44): 14290–14298. doi:10.1021/bi048606d. PMID 15518580.

External links

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