4m4n
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Structural evaluation the Y358H mutant of the aspergillus fumigatus kdnase (sialidase)
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Structural highlights
FunctionSIA_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
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This page was last modified 12:24, 1 March 2024.