Structural highlights
Function
OGA_BACTN Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The synthesis of an analogue of 6-epi-valienamine bearing an acetamido group and its characterisation as an inhibitor of beta-N-acetylglucosaminidases are described. The compound is a good inhibitor of both human O-GlcNAcase and human beta-hexosaminidase, as well as two bacterial beta-N-acetylglucosaminidases. A 3-D structure of the complex of Bacteroides thetaiotaomicron BtGH84 with the inhibitor shows the unsaturated ring is surprisingly distorted away from its favoured solution phase conformation and reveals potential for improved inhibitor potency.
A 1-acetamido derivative of 6-epi-valienamine: an inhibitor of a diverse group of beta-N-acetylglucosaminidases.,Scaffidi A, Stubbs KA, Dennis RJ, Taylor EJ, Davies GJ, Vocadlo DJ, Stick RV Org Biomol Chem. 2007 Sep 21;5(18):3013-9. Epub 2007 Aug 15. PMID:17728868[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Scaffidi A, Stubbs KA, Dennis RJ, Taylor EJ, Davies GJ, Vocadlo DJ, Stick RV. A 1-acetamido derivative of 6-epi-valienamine: an inhibitor of a diverse group of beta-N-acetylglucosaminidases. Org Biomol Chem. 2007 Sep 21;5(18):3013-9. Epub 2007 Aug 15. PMID:17728868 doi:10.1039/b709681j
