Function and Biology Details
Reaction catalysed:
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.
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
exo-alpha-sialidase (preferred)
PDBe Complex ID:
PDB-CPX-186904 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
exo-alpha-sialidase
Molecule details ›
Chain: A
Length: 143 amino acids
Theoretical weight: 15.14 KDa
Source organism: Clostridium perfringens
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: F5/8 type C domain
Structure domains: Galactose-binding domain-like
Length: 143 amino acids
Theoretical weight: 15.14 KDa
Source organism: Clostridium perfringens
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
Q8XMY5 (Residues: 41-180; Coverage: 12%)
Sequence domains: F5/8 type C domain
Structure domains: Galactose-binding domain-like
