Structural highlights
Function
O85361_STRPL
Publication Abstract from PubMed
Mono-, di- and trisaccharide derivatives of 1,2-unsaturated N-acetyl-d-glucal have been synthesized and shown to function as tight-binding inhibitors/slow substrates of representative hexosaminidases. Turnover is slow and not observed in the thioamide analogue, allowing determination of the 3-dimensional structure of the complex. Inhibition is insensitive to pH and to mutation of key catalytic residues, consistent with the uncharged character of the inhibitor. These properties could render this inhibitor class less prone to development of resistance.
N-Acetyl glycals are tight-binding and environmentally insensitive inhibitors of hexosaminidases.,Santana AG, Vadlamani G, Mark BL, Withers SG Chem Commun (Camb). 2016 Jun 28;52(51):7943-6. doi: 10.1039/c6cc02520j. Epub 2016, Jun 2. PMID:27253678[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Santana AG, Vadlamani G, Mark BL, Withers SG. N-Acetyl glycals are tight-binding and environmentally insensitive inhibitors of hexosaminidases. Chem Commun (Camb). 2016 Jun 28;52(51):7943-6. doi: 10.1039/c6cc02520j. Epub 2016, Jun 2. PMID:27253678 doi:http://dx.doi.org/10.1039/c6cc02520j