Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Specificity of substrate recognition by type II dehydroquinases as revealed by binding of polyanions.,Evans LD, Roszak AW, Noble LJ, Robinson DA, Chalk PA, Matthews JL, Coggins JR, Price NC, Lapthorn AJ FEBS Lett. 2002 Oct 23;530(1-3):24-30. PMID:12387860[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. PMID:12387860
