Journal
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
Volume 1800, Issue 2, Pages 122-133Publisher
ELSEVIER
DOI: 10.1016/j.bbagen.2009.07.019
Keywords
Structure; O-GlcNAc; Enzyme; Reaction mechanism; Carbohydrate-active enzyme; GH84; GT41; Hydrolase; Transferase
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Funding
- Biotechnology and Biological Sciences Research Council (BBSRC)
- University of York Wild
- Biotechnology and Biological Sciences Research Council [BB/F007124/1] Funding Source: researchfish
- BBSRC [BB/F007124/1] Funding Source: UKRI
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In order to study the O-GlcNAc modification in vivo, it is evident that a range of specific small molecule inhibitors would be a valuable asset. One strategy for the design of such compounds would be to utilise 3-D structural information in tandem with knowledge of catalytic mechanism. The last few years has seen major breakthroughs in our understanding of the 3-D structure of the enzymes involved in the O-GlcNAc modification notably from the study of the tetratricopeptide repeat (TPR) domain of the human O-GlcNAc transferase, of the bacterial homologs of the O-GlcNAc hydrolase and more latterly bacterial homologs of the O-GlcNAc transferase itself. Of particular note are the bacterial O-GlcNAc hydrolase homologs that provide near identical active centres to the human enzyme. These have informed the design and/or subsequent analysis of inhibitors of this enzyme which have found great use in the chemical dissection of the O-GlcNAc in vivo, as described by Macauley and Vocadlo elsewhere in this issue. (C) 2009 Elsevier B.V. All rights reserved.
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