Structural highlights
Publication Abstract from PubMed
Enzyme transition-state mimics can act as powerful inhibitors and allow structural studies that report on the conformation of the transition-state. Here, mannoimidazole, a mimic of the transition state of mannosidase catalyzed hydrolysis of mannosides, is shown to bind in a B2,5 conformation on the Clostridium perfringens GH125 alpha-1,6-mannosidase, providing additional evidence of a OS2-B2,5-1S5 conformational itinerary for enzymes of this family.
Distortion of mannoimidazole supports a B2,5 boat transition state for the family GH125 alpha-1,6-mannosidase from Clostridium perfringens.,Males A, Speciale G, Williams SJ, Davies GJ Org Biomol Chem. 2019 Aug 13. doi: 10.1039/c9ob01161g. PMID:31407758[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Males A, Speciale G, Williams SJ, Davies GJ. Distortion of mannoimidazole supports a B2,5 boat transition state for the family GH125 alpha-1,6-mannosidase from Clostridium perfringens. Org Biomol Chem. 2019 Aug 13. doi: 10.1039/c9ob01161g. PMID:31407758 doi:http://dx.doi.org/10.1039/c9ob01161g
