The structure and mechanism of the type II dehydroquinase from streptomyces coelicolor

A.W. Roszak, D.A. Robinson, T. Krell, I.S. Hunter, M. Fredrickson, C. Abell, J.R. Coggins, A.J. Lapthorn

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75 Citations (Scopus)


The structure of the type II DHQase from Streptomyces coelicolor has been solved and refined to high resolution in complexes with a number of ligands, including dehydroshikimate and a rationally designed transition state analogue, 2,3-anhydro-quinic acid. These structures define the active site of the enzyme and the role of key amino acid residues and provide snap shots of the catalytic cycle. The resolution of the flexible lid domain (residues 21–31) shows that the invariant residues Arg23 and Tyr28 close over the active site cleft. The tyrosine acts as the base in the initial proton abstraction, and evidence is provided that the reaction proceeds via an enol intermediate. The active site of the structure of DHQase in complex with the transition state analog also includes molecules of tartrate and glycerol, which provide a basis for further inhibitor design.
Original languageEnglish
Pages (from-to)493-503
Number of pages11
Issue number4
Publication statusPublished - 2002


  • shikimate pathway
  • rational drug design
  • enzyme mechanism
  • X-ray structure
  • transition state analog
  • dehydroquinase


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