Download MendeleySpecificity of Substrate Recognition by Type II Dehydroquinases as Revealed by Binding of Polyanions(1)
Evans, L., Roszak, A.W., Noble, L., Robinson, D., Chalk, P., Matthews, J., Coggins, J.R., Price, N., Lapthorn, A.J.(2002) FEBS Lett 530: 24
- PubMed: 12387860
- DOI: https://doi.org/10.1016/s0014-5793(02)03346-x
- Primary Citation of Related Structures:
1H05 - PubMed 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.
Organizational Affiliation:
Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, University of Glasgow, UK.
