Distortion of mannoimidazole supports a B2, 5 boat transition state for the family GH125 α-1, 6-mannosidase from Clostridium perfringens. Issue 34 (13th August 2019)

• Record Type: Journal Article
• Authors: Males, Alexandra; Speciale, Gaetano; Williams, Spencer J.; Davies, Gideon J.
• Is Part Of: Organic & biomolecular chemistry. Volume 17:Issue 34(2019)
• Page Start: 7863
• Page End: 7869
• Publication Date: 2019-08-13
• Subjects: Chemistry, Organic -- Periodicals; Bioorganic chemistry -- Periodicals; Chemistry, Physical organic -- Periodicals; 547
• DOI: 10.1039/c9ob01161g
• Languages: English
• ISSNs: 1477-0520

Abstract

Abstract : Enzyme transition-state mimics can act as powerful inhibitors and allow structural studies that report on the conformation of the transition-state. Abstract : 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 B 2, 5 conformation on the Clostridium perfringens GH125 α-1, 6-mannosidase, providing additional evidence of a O S 2 – B 2, 5 – 1 S 5 conformational itinerary for enzymes of this family.