FEBS Letters
Volume 579, Issue 2 , Pages 302-312, 17 January 2005

An elaboration on the syn–anti proton donor concept of glycoside hydrolases: electrostatic stabilisation of the transition state as a general strategy

Edited by Stuart Ferguson

  • W. Nerinckx

      Affiliations

    • Corresponding Author InformationCorresponding author. Fax: +32 9 264 5332
    • ,
  • T. Desmet
    • ,
  • K. Piens

      Affiliations

    • Present address: Laboratory of Wood Biotechnology, Royal Institute of Technology, AlbaNova University Centre, KTH Biotechnology, SE-106 91 Stockholm, Sweden.
    • ,
  • M. Claeyssens

Laboratory for Glycobiology, Department of Biochemistry, Physiology and Microbiology, Ghent University, K.L. Ledeganckstraat 35, B-9000 Gent, Belgium

Received 29 October 2004; received in revised form 10 December 2004; accepted 10 December 2004. published online 22 December 2004.

Abstract 

An in silico survey of all known 3D-structures of glycoside hydrolases that contain a ligand in the −1 subsite is presented. A recurrent crucial positioning of active site residues indicates a common general strategy for electrostatic stabilisation directed to the carbohydrate’s ring-oxygen at the transition state. This is substantially different depending on whether the enzyme’s proton donor is syn or anti positioned versus the substrate. A comprehensive list of enzymes belonging to 42 different families is given and selected examples are described. An implication for an early evolution scenario of glycoside hydrolases is discussed.

Keywords: Glycoside hydrolase, Substrate/ligand complex, Enzyme mechanism

 

PII: S0014-5793(04)01556-X

doi:10.1016/j.febslet.2004.12.021

FEBS Letters
Volume 579, Issue 2 , Pages 302-312, 17 January 2005

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