Specificity of substrate recognition by type II dehydroquinases as revealed by binding of polyanions.
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Evans LD, Roszak AW, Noble LJ, Robinson DA, Chalk PA, Matthews JL, Coggins JR, Price NC, Lapthorn AJ
Specificity of substrate recognition by type II dehydroquinases as revealed by binding of polyanions.
FEBS Lett. 2002 Oct 23;530(1-3):24-30.
- PubMed ID
- 12387860 [ View in 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.