Visualizing the Reaction Coordinate of an O-GlcNAc Hydrolase | Zendy

Yuan He | Zendy; Matthew S. Macauley | Zendy; Keith A. Stubbs | Zendy; David J. Vocadlo | Zendy; G.J. Davies | Zendy

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Visualizing the Reaction Coordinate of an O-GlcNAc Hydrolase

Author(s) -

Yuan He,

Matthew S. Macauley,

Keith A. Stubbs,

David J. Vocadlo,

G.J. Davies

Publication year - 2010

Publication title -

journal of the american chemical society

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 7.115

H-Index - 612

eISSN - 1520-5126

pISSN - 0002-7863

DOI - 10.1021/ja9086769

Subject(s) - chemistry , oxazoline , threonine , serine , hydrolase , substrate (aquarium) , reaction coordinate , biochemistry , substrate specificity , catalysis , mechanism (biology) , stereochemistry , phosphorylation , enzyme , computational chemistry , oceanography , philosophy , epistemology , geology

N-Acetylglucosamine beta-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.

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