4m4v: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4m4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m4v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m4v RCSB], [http://www.ebi.ac.uk/pdbsum/4m4v PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4m4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m4v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m4v RCSB], [http://www.ebi.ac.uk/pdbsum/4m4v PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/SIA_ASPFU 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.<ref>PMID:20652740</ref> | |||
== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
