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Distortion of mannoimidazole supports a B 2,5 boat transition state for the family GH125 α-1,6-mannosidase from Clostridium perfringens
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.
Subject Areas:
Biology and Bio-materials,
Chemistry
Instruments:
I24-Microfocus Macromolecular Crystallography
Documents:
hgj66u.pdf
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