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Specificity of substrate recognition by type II dehydroquinases as revealed by binding of polyanions11 The atomic coordinates have been deposited in the Protein Data Bank with the accession code 1H05.

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
530
Identifiers
DOI: 10.1016/s0014-5793(02)03346-x
Keywords
  • Dehydroquinase
  • 3-Dehydroquinic Acid
  • Substrate Recognition
  • X-Ray Crystallography
  • Phosphate
  • Sulfate
Disciplines
  • Biology
  • Design

Abstract

Abstract The interactions between the polyanionic ligands phosphate and sulphate and the type II dehydroquinases from Streptomyces coelicolor and Mycobacterium tuberculosis have been characterised using a combination of structural and kinetic methods. From both approaches, it is clear that interactions are more complex in the case of the latter enzyme. The data provide new insights into the differences between the two enzymes in terms of substrate recognition and catalytic efficiency and may also explain the relative potencies of rationally designed inhibitors. An improved route to the synthesis of the substrate 3-dehydroquinic acid (dehydroquinate) is described.

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