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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
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
UDP-N-acetylglucosamine 2-epimerase
crystal structure of udp-n-acetylglucosamine_2 epimerase
Identifiers
SymbolEpimerase_2
PfamPF02350
Pfam clanCL0113
InterProIPR003331
SCOP21f6d / SCOPe / SUPFAM
CDDcd03786
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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

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

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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

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Notes

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

References

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  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

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