UDP-N-acetylglucosamine 4-epimerase
In enzymology, an UDP-N-acetylglucosamine 4-epimerase (EC 5.1.3.7) is an enzyme that catalyzes the chemical reaction
- UDP-N-acetyl-D-glucosamine UDP-N-acetyl-D-galactosamine
UDP-N-acetylglucosamine 4-epimerase | |||||||||
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Identifiers | |||||||||
EC number | 5.1.3.7 | ||||||||
CAS number | 9024-16-2 | ||||||||
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 | ||||||||
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Hence, this enzyme has one substrate, UDP-N-acetyl-D-glucosamine, and one product, UDP-N-acetyl-D-galactosamine.
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 4-epimerase. Other names in common use include UDP acetylglucosamine epimerase, uridine diphosphoacetylglucosamine epimerase, uridine diphosphate N-acetylglucosamine-4-epimerase, and uridine 5'-diphospho-N-acetylglucosamine-4-epimerase. This enzyme participates in aminosugars metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1SB8 and 1SB9.
References
- Glaser L (November 1959). "The biosynthesis of N-acetylgalactosamine". The Journal of Biological Chemistry. 234: 2801–5. PMID 13828347.
- Kornfeld S, Glaser L (October 1962). "The synthesis of thymidine-linked sugars. v. thymidine diphosphate-amino sugars". The Journal of Biological Chemistry. 237: 3052–9. PMID 14034827.