Distortion of mannoimidazole supports a B 2,5 boat transition state for the family GH125 α-1,6-mannosidase from Clostridium perfringens

DOI: 10.1039/C9OB01161G

Authors: Alexandra Males (The University of York) , Gaetano Speciale (University of Melbourne) , Spencer J. Williams (University of Melbourne) , Gideon J. Davies (The University of York)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Organic & Biomolecular Chemistry , VOL 45

State: Published (Approved)
Published: August 2019
Diamond Proposal Number(s): 9948

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 B2,5 conformation on the Clostridium perfringens GH125 α-1,6-mannosidase, providing additional evidence of a OS2–B2,5–1S5 conformational itinerary for enzymes of this family.

Diamond Keywords: Enzymes

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I24-Microfocus Macromolecular Crystallography

Added On: 28/08/2019 10:15

Documents:
hgj66u.pdf

Discipline Tags:

Biochemistry Catalysis Chemistry Structural biology Organic Chemistry Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)