UDP-N-acetylglucosamine 2-epimerase
In enzymology, an UDP-N-acetylglucosamine 2-epimerase (EC 5.1.3.14) is an enzyme that catalyzes the chemical reaction
- UDP-N-acetyl-D-glucosamine UDP-N-acetyl-D-mannosamine
| UDP-N-acetylglucosamine 2-epimerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 5.1.3.14 | ||||||||
| CAS number | 9037-71-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| UDP-N-acetylglucosamine 2-epimerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of udp-n-acetylglucosamine_2 epimerase | |||||||||
| Identifiers | |||||||||
| Symbol | Epimerase_2 | ||||||||
| Pfam | PF02350 | ||||||||
| Pfam clan | CL0113 | ||||||||
| InterPro | IPR003331 | ||||||||
| SCOP2 | 1f6d / SCOPe / SUPFAM | ||||||||
| CDD | cd03786 | ||||||||
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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.
References
- 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.
- 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.
- 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
- Kikuchi K, Tsuiki S (1973). "Purification and properties of UDP-N-acetylglucosamine 2'-epimerase from rat liver". Biochim. Biophys. Acta. 327 (1): 193–206. doi:10.1016/0005-2744(73)90117-4. PMID 4770741.