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Visualizing the Reaction Coordinate of an O-GlcNAc Hydrolase

DOI: 10.1021/ja9086769 DOI Help
PMID: 20067256 PMID Help

Authors: Yuan He (University of York) , Matthew S. Macauley (Simon Fraser University) , Keith A. Stubbs (Simon Fraser University; University of Western Australia) , David J. Vocadlo (Simon Fraser University) , Gideon J. Davies (University of York)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of The American Chemical Society , VOL 132 (6)

State: Published (Approved)
Published: January 2010

Abstract: N-Acetylglucosamine β-O-linked to serine and threonine residues of nucleocytoplasmic proteins (O-GlcNAc) has been linked to neurodegeneration, cellular stress response, and transcriptional regulation. Removal of O-GlcNAc is catalyzed by O-GlcNAcase (OGA) using a substrate-assisted catalytic mechanism. Here we define the reaction coordinate using chemical approaches and directly observe both a Michaelis complex and the oxazoline intermediate.

Journal Keywords: Biocatalysis; Electron; Humans; Hydrolases; Models; Molecular; Oxazoles; Protein Conformation

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography

Added On: 01/10/2010 12:02

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