Specificity of substrate recognition by type II dehydroquinases as revealed by binding of polyanions

Evans, L. D.B., Roszak, A. W., Noble, L. J., Robinson, D. A., Chalk, P. A., Matthews, J. L., Coggins, J. R., Price, N. C. and Lapthorn, A. J. (2002) Specificity of substrate recognition by type II dehydroquinases as revealed by binding of polyanions. FEBS Letters, 530(1-3), pp. 24-30. (doi: 10.1016/S0014-5793(02)03346-X)

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Abstract

The interactions between the polyanionic ligands phosphate and sulphate and the type II dehydroquinases from <i>Streptomyces coelicolor</i> and <i>Mycobacterium tuberculosis</i> 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.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Lapthorn, Dr Adrian and Price, Prof Nicholas and Coggins, Professor John and Roszak, Dr Aleksander
Authors: Evans, L. D.B., Roszak, A. W., Noble, L. J., Robinson, D. A., Chalk, P. A., Matthews, J. L., Coggins, J. R., Price, N. C., and Lapthorn, A. J.
Subjects:Q Science > QH Natural history > QH345 Biochemistry
College/School:College of Medical Veterinary and Life Sciences
College of Science and Engineering > School of Chemistry
Journal Name:FEBS Letters
Publisher:Elsevier BV
ISSN:0014-5793
ISSN (Online):1873-3468
Published Online:26 September 2002

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