Specificity of substrate recognition by type II dehydroquinases as revealed by binding of polyanions.
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.
Evans
Lewis D B
LD
Division of Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, University of Glasgow, UK.
Roszak
Aleksander W
AW
Noble
Lorna J
LJ
Robinson
David A
DA
Chalk
Peter A
PA
Matthews
Jennifer L
JL
Coggins
John R
JR
Price
Nicholas C
NC
Lapthorn
Adrian J
AJ
D018360:Crystallography, X-Ray; D006836:Hydro-Lyases / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D009169:Mycobacterium tuberculosis / Q000201:enzymology; D019906:Nuclear Magnetic Resonance, Biomolecular; D000071228:Polyelectrolytes; D011108:Polymers / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D013302:Streptomyces / Q000201:enzymology; D013379:Substrate Specificity
D006836:Hydro-Lyases; D000071228:Polyelectrolytes; D011108:Polymers; C020000:3-dehydroquinate dehydratase