In enzymology, an UDP-N-acetylglucosamine 4-epimerase (EC 5.1.3.7) is an enzyme that catalyzes the chemical reaction
UDP-N-acetylglucosamine 4-epimerase | |||||||||
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Identifiers | |||||||||
EC no. | 5.1.3.7 | ||||||||
CAS no. | 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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- UDP-N-acetyl-D-glucosamine UDP-N-acetyl-D-galactosamine
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
editAs of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1SB8 and 1SB9.
References
edit- Glaser L (November 1959). "The biosynthesis of N-acetylgalactosamine". The Journal of Biological Chemistry. 234 (11): 2801–5. doi:10.1016/S0021-9258(18)69673-5. 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 (10): 3052–9. doi:10.1016/S0021-9258(18)50119-8. PMID 14034827.