Structural highlights
Function
SIA_ASPFU Sialidase is able to release sialic acid from a wide variety of natural substrates including bovine salivary mucin, colominic acid, bovine fetuin, a serum glycoprotein containing both alpha-2-6 and alpha-2-3-linkages in a ratio of about 3:2, and glycoproteins and glycolipids from thermally denatured human lung epithelial cells. Does not show any trans-sialidase activity since it is able to remove terminal sialic acid residues but is unable to catalyze their transfer to the acceptor substrate. 2-keto-3-deoxynononic acid (KDN) is the preferred substrate and A.fumigatus can utilize KDN as a sole carbon source.[1]
References
- ↑ Warwas ML, Yeung JH, Indurugalla D, Mooers AO, Bennet AJ, Moore MM. Cloning and characterization of a sialidase from the filamentous fungus, Aspergillus fumigatus. Glycoconj J. 2010 Jul;27(5):533-48. doi: 10.1007/s10719-010-9299-9. Epub 2010 Jul, 23. PMID:20652740 doi:http://dx.doi.org/10.1007/s10719-010-9299-9
