Structural analyses of enzymes involved in the O-GlcNAc modification

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JournalBIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
DatePublished - Feb 2010
Issue number2
Volume1800
Number of pages12
Pages (from-to)122-133
Original languageEnglish

Abstract

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.

    Research areas

  • Structure, O-GlcNAc, Enzyme, Reaction mechanism, Carbohydrate-active enzyme, GH84, GT41, Hydrolase, Transferase, BETA-N-ACETYLGLUCOSAMINIDASE, SUBSTRATE-ASSISTED CATALYSIS, TAY-SACHS-DISEASE, LINKED GLCNAC, CRYSTAL-STRUCTURE, GLYCOSIDE HYDROLASES, FUNCTIONAL-ANALYSIS, NUCLEOCYTOPLASMIC PROTEINS, TETRATRICOPEPTIDE REPEATS, SELECTIVE-INHIBITION

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