UDP-N-acetylglucosamine 2-epimerase

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UDP-N-acetylglucosamine 2-epimerase
Identifiers
EC no. 5.1.3.14
CAS no. 9037-71-2
Databases
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BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
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NCBI proteins
UDP-N-acetylglucosamine 2-epimerase
PDB 1vgv EBI.jpg
crystal structure of udp-n-acetylglucosamine_2 epimerase
Identifiers
SymbolEpimerase_2
Pfam PF02350
Pfam clan CL0113
InterPro IPR003331
SCOP2 1f6d / SCOPe / SUPFAM
CDD cd03786
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

In enzymology, an UDP-N-acetylglucosamine 2-epimerase [note 1] (EC 5.1.3.14) is an enzyme that catalyzes the chemical reaction

Contents

UDP-N-acetyl-D-glucosamine UDP-N-acetyl-D-mannosamine

Hence, this enzyme has one substrate, UDP-N-acetyl-D-glucosamine, and one product, UDP-N-acetyl-D-mannosamine.

This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on carbohydrates and derivatives. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine 2-epimerase. Other names in common use include UDP-N-acetylglucosamine 2'-epimerase, uridine diphosphoacetylglucosamine 2'-epimerase, uridine diphospho-N-acetylglucosamine 2'-epimerase, and uridine diphosphate-N-acetylglucosamine-2'-epimerase. This enzyme participates in aminosugars metabolism.

In microorganisms this epimerase is involved in the synthesis of the capsule precursor UDP-ManNAcA. [1] [2] An inhibitor of the bacterial 2-epimerase, epimerox, has been described. Some of these enzymes are bifunctional. The UDP-N-acetylglucosamine 2-epimerase from rat liver displays both epimerase and kinase activity. [3]

Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1F6D, 1O6C, 1V4V, and 1VGV.

See also

Notes

  1. Not to be confused with N-acetylglucosamine 2-epimerase

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).

In enzymology, an UDP-N-acetylglucosamine 6-dehydrogenase (EC 1.1.1.136) is an enzyme that catalyzes the chemical reaction

<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-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, a protein 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

In enzymology, an UDP-galactose—UDP-N-acetylglucosamine galactose phosphotransferase 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">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.

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

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

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). This enzyme catalyses the following chemical reaction

References

  1. Swartley JS, Liu LJ, Miller YK, Martin LE, Edupuganti S, Stephens DS (March 1998). "Characterization of the Gene Cassette Required for Biosynthesis of the (α1→6)-Linked N-Acetyl-d-Mannosamine-1-Phosphate Capsule of Serogroup A Neisseria meningitidis". J. Bacteriol. 180 (6): 1533–9. doi:10.1128/JB.180.6.1533-1539.1998. PMC   107054 . PMID   9515923.
  2. Kiser KB, Lee JC (January 1998). "Staphylococcus aureus cap5O and cap5P Genes Functionally Complement Mutations Affecting Enterobacterial Common-Antigen Biosynthesis in Escherichia coli". J. Bacteriol. 180 (2): 403–6. doi:10.1128/JB.180.2.403-406.1998. PMC   106897 . PMID   9440531.
  3. Stasche 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". J. Biol. Chem. 272 (39): 24319–24. doi: 10.1074/jbc.272.39.24319 . PMID   9305888.

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR003331