N-acetylneuraminate epimerase (EC 5.1.3.24, sialic acid epimerase, N-acetylneuraminate mutarotase, sialic acid mutarotase, YjhT, NanM) is an enzyme with systematic name N-acetyl-alpha-neuraminate 2-epimerase.[1] This enzyme catalyses the following chemical reaction
| N-acetylneuraminate epimerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.1.3.24 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- N-acetyl-alpha-neuraminate N-acetyl-beta-neuraminate
Sialoglycoconjugates present in vertebrates are linked exclusively by alpha-linkages.
See also
editReferences
edit- ^ Severi E, Müller A, Potts JR, Leech A, Williamson D, Wilson KS, Thomas GH (February 2008). "Sialic acid mutarotation is catalyzed by the Escherichia coli beta-propeller protein YjhT". The Journal of Biological Chemistry. 283 (8): 4841–9. doi:10.1074/jbc.M707822200. PMID 18063573.
External links
edit- N-acetylneuraminate+epimerase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
