N-acylglucosamine 2-epimerase
| N-acylglucosamine 2-epimerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 N-acylglucosamine 2-epimerase dimer, Sus scrofa | |||||||||
| Identifiers | |||||||||
| EC no. | 5.1.3.8 | ||||||||
| CAS no. | 37318-34-6 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a N-acylglucosamine 2-epimerase (EC 5.1.3.8) is an enzyme that catalyzes the chemical reaction
- N-acyl-D-glucosamine N-acyl-D-mannosamine
Hence, this enzyme has one substrate, N-acyl-D-glucosamine, and one product, N-acyl-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 N-acyl-D-glucosamine 2-epimerase. Other names in common use include acylglucosamine 2-epimerase, and N-acetylglucosamine 2-epimerase. This enzyme participates in aminosugars metabolism. It employs one cofactor, ATP.
Structural studies
As of late 2019, three structures have been solved for this class of enzymes, with the PDB accession codes PDB: 1FP3, PDB: 2GZ6, and PDB: 6F04. They show that the N-acylglucosamine 2-epimerase monomer folds as a barrel composed of α-helices, in a manner known as (α/α)6-barrel. The structures are presented as dimers, with the structures from Sus scrofa and Anabaena sp. CH1 having a different organization than the structure from Nostoc sp. KJV10.
References
- Ghosh S, Roseman S (April 1965). "The sialic acids. V. N-Acyl-D-glucosamine 2-epimerase". The Journal of Biological Chemistry. 240: 1531–6. doi:10.1016/S0021-9258(18)97468-5. PMID 14285488.