Uridine diphosphate N-acetylglucosamine

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Uridine diphosphate N-acetylglucosamine
UDP-N-acetylglucosamine.png
Names
IUPAC name
Uridine 5′-(2-acetamido-2-deoxy-α-D-glucopyranosyl dihydrogen diphosphate)
Systematic IUPAC name
O1-[(2R,3R,4R,5S,6R)-3-Acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl] O3-{[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxyoxolan-2-yl]methyl} dihydrogen diphosphate
Other names
UDP-N-acetylglucosamine; UDP-GlcNAc
Identifiers
3D model (JSmol)
PubChem CID
  • CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@@H]1OP(=O)(O)OP(=O)(O)OC[C@@H]2[C@H]([C@H]([C@@H](O2)N3C=CC(=O)NC3=O)O)O)CO)O)O
Properties
C17H27N3O17P2
Molar mass 607.355 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Uridine diphosphate N-acetylglucosamine or UDP-GlcNAc is a nucleotide sugar and a coenzyme in metabolism. It is used by glycosyltransferases to transfer N-acetylglucosamine residues to substrates. D-Glucosamine is made naturally in the form of glucosamine-6-phosphate, and is the biochemical precursor of all nitrogen-containing sugars. [1] To be specific, glucosamine-6-phosphate is synthesized from fructose 6-phosphate and glutamine [2] as the first step of the hexosamine biosynthesis pathway. [3] The end-product of this pathway is UDP-GlcNAc, which is then used for making glycosaminoglycans, proteoglycans, and glycolipids. [4]

UDP-GlcNAc is extensively involved in intracellular signaling as a substrate for O-linked N-acetylglucosamine transferases (OGTs) to install the O-GlcNAc post-translational modification in a wide range of species. It is also involved in nuclear pore formation and nuclear signalling. OGTs and OG-ases play an important role in the structure of the cytoskeleton. In mammals, there is enrichment of OGT transcripts in the pancreas beta-cells, and UDP-GlcNAc is thought to be part of the glucose sensing mechanism. There is also evidence that it plays a part in insulin sensitivity in other cells. In plants, it is involved in the control of gibberellin production. [5]

Clostridium novyi type A alpha-toxin is an O-linked N-actetylglucosamine transferase acting on Rho proteins and causing the collapse of the cytoskeleton.

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-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.

Nucleotide sugars are the activated forms of monosaccharides. Nucleotide sugars act as glycosyl donors in glycosylation reactions. Those reactions are catalyzed by a group of enzymes called glycosyltransferases.

<span class="mw-page-title-main">N-acetylglucosamine-6-phosphate deacetylase</span>

In enzymology, N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25), also known as GlcNAc-6-phosphate deacetylase or NagA, is an enzyme that catalyzes the deacetylation of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to glucosamine-6-phosphate (GlcN-6-P):

<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 protein N-acetylglucosaminyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a [Skp1-protein]-hydroxyproline 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">UDP-N-acetylglucosamine diphosphorylase</span> Class of enzymes

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

<span class="mw-page-title-main">DPAGT1</span> Protein-coding gene in the species Homo sapiens

UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase is an enzyme that in humans is encoded by the DPAGT1 gene.

Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-glucosamine:O-glycosyl-glycoprotein 6-beta-N-acetyl-D-glucosaminyltransferase. This enzyme catalyses the following chemical reaction

N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-glucosamine:N-acetyl-D-glucosaminyl-diphosphodolichol 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—undecaprenyl-phosphate N-acetylglucosaminephosphotransferase is an enzyme with systematic name UDP-N-acetyl-alpha-D-glucosamine:ditrans,octacis-undecaprenyl phosphate N-acetyl-alpha-D-glucosaminephosphotransferase. This enzyme catalyses the following chemical reaction

UDP-N-acetylglucosamine---decaprenyl-phosphate N-acetylglucosaminephosphotransferase is an enzyme with systematic name UDP-N-acetyl-alpha-D-glucosamine:trans,octacis-decaprenyl-phosphate N-acetylglucosaminephosphotransferase. This enzyme catalyses the following chemical reaction

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

Protein O-GlcNAcase (EC 3.2.1.169, OGA, glycoside hydrolase O-GlcNAcase, O-GlcNAcase, BtGH84, O-GlcNAc hydrolase) is an enzyme with systematic name (protein)-3-O-(N-acetyl-D-glucosaminyl)-L-serine/threonine N-acetylglucosaminyl hydrolase. OGA is encoded by the OGA gene. This enzyme catalyses the removal of the O-GlcNAc post-translational modification in the following chemical reaction:

  1. [protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-serine + H2O ⇌ [protein]-L-serine + N-acetyl-D-glucosamine
  2. [protein]-3-O-(N-acetyl-β-D-glucosaminyl)-L-threonine + H2O ⇌ [protein]-L-threonine + N-acetyl-D-glucosamine

UDP-3-O-acyl-N-acetylglucosamine deacetylase (EC 3.5.1.108, LpxC protein, LpxC enzyme, LpxC deacetylase, deacetylase LpxC, UDP-3-O-acyl-GlcNAc deacetylase, UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase, UDP-(3-O-acyl)-N-acetylglucosamine deacetylase, UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase, UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase) is an enzyme with systematic name UDP-3-O-((3R)-3-hydroxymyristoyl)-N-acetylglucosamine amidohydrolase. This enzyme catalyses the following chemical reaction

<i>O</i>-GlcNAc

O-GlcNAc is a reversible enzymatic post-translational modification that is found on serine and threonine residues of nucleocytoplasmic proteins. The modification is characterized by a β-glycosidic bond between the hydroxyl group of serine or threonine side chains and N-acetylglucosamine (GlcNAc). O-GlcNAc differs from other forms of protein glycosylation: (i) O-GlcNAc is not elongated or modified to form more complex glycan structures, (ii) O-GlcNAc is almost exclusively found on nuclear and cytoplasmic proteins rather than membrane proteins and secretory proteins, and (iii) O-GlcNAc is a highly dynamic modification that turns over more rapidly than the proteins which it modifies. O-GlcNAc is conserved across metazoans.

References

  1. ↑ Roseman, S (2001). "Reflections on glycobiology". The Journal of Biological Chemistry. 276 (45): 41527–42. doi: 10.1074/jbc.R100053200 . PMID   11553646.
  2. ↑ Sudhamoy Ghosh; Blumenthal, HJ; Davidson, E; Roseman, S (1960-05-01). "Glucosamine Metabolism". Journal of Biological Chemistry. 235 (5): 1265–73. PMID   13827775.
  3. ↑ International Union of Biochemistry and Molecular Biology
  4. ↑ Milewski S, Gabriel I, Olchowy J (2006). "Enzymes of UDP-GlcNAc biosynthesis in yeast". Yeast. 23 (1): 1–14. doi: 10.1002/yea.1337 . PMID   16408321.
  5. ↑ Hanover, J. A. (2001). "Glycan-dependent signaling: O-linked N-acetylglucosamine". The FASEB Journal. 15 (11): 1865–1876. CiteSeerX   10.1.1.324.6370 . doi:10.1096/fj.01-0094rev. PMID   11532966.
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