5foo: 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=5foo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5foo OCA], [http://pdbe.org/5foo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5foo RCSB], [http://www.ebi.ac.uk/pdbsum/5foo 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=5foo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5foo OCA], [http://pdbe.org/5foo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5foo RCSB], [http://www.ebi.ac.uk/pdbsum/5foo PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Covalent, mechanism-based inhibitors of glycosidases are valuable probe molecules for visualizing enzyme activities in complex systems. We, here, describe the chemoenzymatic synthesis of 6-phospho-cyclophellitol and evaluate its behaviour as a mechanism-based inactivator of the Streptococcus pyogenes 6-phospho-beta-glucosidase from CAZy family GH1. We further present the three-dimensional structure of the inactivated enzyme, which reveals the constellation of active site residues responsible for the enzyme's specificity and confirms the covalent nature of the inactivation. | |||
Chemoenzymatic synthesis of 6-phospho-cyclophellitol as a novel probe of 6-phospho-beta-glucosidases.,Kwan DH, Jin Y, Jiang J, Chen HM, Kotzler MP, Overkleeft HS, Davies GJ, Withers SG FEBS Lett. 2016 Feb;590(4):461-8. doi: 10.1002/1873-3468.12059. Epub 2016 Feb 14. PMID:26790390<ref>PMID:26790390</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5foo" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:04, 2 March 2016
6-phospho-beta-glucosidase6-phospho-beta-glucosidase
Structural highlights
Publication Abstract from PubMedCovalent, mechanism-based inhibitors of glycosidases are valuable probe molecules for visualizing enzyme activities in complex systems. We, here, describe the chemoenzymatic synthesis of 6-phospho-cyclophellitol and evaluate its behaviour as a mechanism-based inactivator of the Streptococcus pyogenes 6-phospho-beta-glucosidase from CAZy family GH1. We further present the three-dimensional structure of the inactivated enzyme, which reveals the constellation of active site residues responsible for the enzyme's specificity and confirms the covalent nature of the inactivation. Chemoenzymatic synthesis of 6-phospho-cyclophellitol as a novel probe of 6-phospho-beta-glucosidases.,Kwan DH, Jin Y, Jiang J, Chen HM, Kotzler MP, Overkleeft HS, Davies GJ, Withers SG FEBS Lett. 2016 Feb;590(4):461-8. doi: 10.1002/1873-3468.12059. Epub 2016 Feb 14. PMID:26790390[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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