UDP-N-acetylglucosamine 2-epimerase (hydrolysing)

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UDP-N-acetylglucosamine 2-epimerase (hydrolysing)
Identifiers
EC no. 3.2.1.183
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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 .

Related Research Articles

<i>N</i>-Acetylmannosamine Chemical compound

N-Acetylmannosamine is a hexosamine monosaccharide. It is a neutral, stable naturally occurring compound. N-Acetylmannosamine is also known as N-Acetyl-D-mannosamine monohydrate,, N-Acetyl-D-mannosamine which can be abbreviated to ManNAc or, less commonly, NAM). ManNAc is the first committed biological precursor of N-acetylneuraminic acid. Sialic acids are the negatively charged, terminal monosaccharides of carbohydrate chains that are attached to glycoproteins and glycolipids (glycans).

<span class="mw-page-title-main">UDP-N-acetylmuramate dehydrogenase</span> Class of enzymes

In enzymology, an UDP-N-acetylmuramate dehydrogenase (EC 1.3.1.98) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">UDP-glucose 4-epimerase</span> Class of enzymes

The enzyme UDP-glucose 4-epimerase, also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity.

<span class="mw-page-title-main">UDP-N-acetylglucosamine 2-epimerase</span> Class of enzymes

In enzymology, an UDP-N-acetylglucosamine 2-epimerase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">UDP-N-acetylglucosamine 4-epimerase</span> Class of enzymes

In enzymology, an UDP-N-acetylglucosamine 4-epimerase is an enzyme that catalyzes the chemical reaction

In enzymology, a glucosamine-1-phosphate N-acetyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Glucosamine-phosphate N-acetyltransferase</span>

In enzymology, glucosamine-phosphate N-acetyltransferase (GNA) is an enzyme that catalyzes the transfer of an acetyl group from acetyl-CoA to the primary amine in glucosamide-6-phosphate, generating a free CoA and N-acetyl-D-glucosamine-6-phosphate.

<span class="mw-page-title-main">UDP-N-acetylglucosamine 1-carboxyvinyltransferase</span> Class of enzymes

In enzymology, an UDP-N-acetylglucosamine 1-carboxyvinyltransferase is an enzyme that catalyzes the first committed step in peptidoglycan biosynthesis of bacteria:

In enzymology, a dolichyl-phosphate alpha-N-acetylglucosaminyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a lipopolysaccharide N-acetylglucosaminyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a phosphatidylinositol N-acetylglucosaminyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, an UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase is an enzyme that catalyzes the chemical reaction

In enzymology, an UDP-N-acetylglucosamine—lysosomal-enzyme N-acetylglucosaminephosphotransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">GNE (gene)</span> Protein-coding gene in humans

Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase is an enzyme that in humans is encoded by the GNE gene.

<span class="mw-page-title-main">RENBP</span> Mammalian protein found in Homo sapiens

N-acylglucosamine 2-epimerase is an enzyme that in humans is encoded by the RENBP gene.

N-acetyl-D-glucosamine kinase is an enzyme that in humans is encoded by the NAGK gene.

Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-glucosamine:6-(alpha-D-mannosyl)-beta-D-mannosyl-glycoprotein 2-beta-N-acetyl-D-glucosaminyltransferase. This enzyme catalyses the following chemical reaction

Protein <i>O</i>-GlcNAc transferase Protein-coding gene in the species Homo sapiens

Protein O-GlcNAc transferase also known as OGT or O-linked N-acetylglucosaminyltransferase is an enzyme that in humans is encoded by the OGT gene. OGT catalyzes the addition of the O-GlcNAc post-translational modification to proteins.

UDP-N-acetylglucosamine kinase is an enzyme with systematic name ATP:UDP-N-acetyl-alpha-D-glucosamine 3'-phosphotransferase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Epimerox</span> Chemical compound

Epimerox is an experimental broad-spectrum antibiotic compound being developed by scientists at the Rockefeller University and Astex Pharmaceuticals. It is a small molecule inhibitor compound that blocks the activity of the enzyme UDP-N-acetylglucosamine 2-epimerase, an epimerase enzyme that is called 2-epimerase for short.

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.