UDP-N-acetylglucosamine 2-epimerase (hydrolysing)
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
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
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