CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.120 | 6 Propeller |
|
2.120.10 | Neuraminidase |
|
2.120.10.10 |
Domain Context
CATH Clusters
| Superfamily | 2.120.10.10 |
| Functional Family | Neuraminidase 3 |
Enzyme Information
| 3.2.1.18 |
Exo-alpha-sialidase.
based on mapping to UniProt Q9Y3R4
Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
-!- The enzyme does not act on 4-O-acetylated sialic acids. -!- An endo-alpha-sialidase activity is listed as EC 3.2.1.129. -!- See also EC 4.2.2.15.
|
UniProtKB Entries (1)
| Q9Y3R4 |
NEUR2_HUMAN
Homo sapiens
Sialidase-2
|
PDB Structure
| PDB | 1VCU |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal Structure of the Human Cytosolic Sialidase Neu2: EVIDENCE FOR THE DYNAMIC NATURE OF SUBSTRATE RECOGNITION
J.Biol.Chem.
|
