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
The recent recrudescence of Mycobacterium tuberculosis infection and the emergence of multidrug-resi...
The enzyme 3-dehydroquinase was purified over 4000-fold to homogeneity from Streptomyces coelicolor....
Structural, biochemical and computational studies to study substrate binding and the role of the con...
AbstractThe interactions between the polyanionic ligands phosphate and sulphate and the type II dehy...
The structure of the type II DHQase from Streptomyces coelicolor has been solved and refined to high...
AbstractThe structure of the type II DHQase from Streptomyces coelicolor has been solved and refined...
The shikimate pathway is essential in Mycobacterium tuberculosis and its absence from humans makes t...
The enzyme 3-dehydroquinase (3-dehydroquinate dehydratase; E.C. 4.2.1.10) catalyses the dehydration ...
The in silico design, synthesis, and biological evaluation of ten potent type II dehydroquinase inhi...
Dehydroquinate synthase (DHQS) is a potential target for the development of novel broad-spectrum ant...
The structural changes caused by the substitution of the aromatic moiety in (2<i>S</i>)-2-benzyl-3-d...
The crystal structures of the type II dehydroquinase (DHQase) from Helicobacter pylori in complex wi...
Structural and computational studies to explore the WAT1 binding pocket in the structure-based desig...
SIGLEAvailable from British Library Document Supply Centre-DSC:DXN020422 / BLDSC - British Library D...
The structures of enzymes catalyzing the reactions in central metabolic pathways are generally well...
The recent recrudescence of Mycobacterium tuberculosis infection and the emergence of multidrug-resi...
The enzyme 3-dehydroquinase was purified over 4000-fold to homogeneity from Streptomyces coelicolor....
Structural, biochemical and computational studies to study substrate binding and the role of the con...
AbstractThe interactions between the polyanionic ligands phosphate and sulphate and the type II dehy...
The structure of the type II DHQase from Streptomyces coelicolor has been solved and refined to high...
AbstractThe structure of the type II DHQase from Streptomyces coelicolor has been solved and refined...
The shikimate pathway is essential in Mycobacterium tuberculosis and its absence from humans makes t...
The enzyme 3-dehydroquinase (3-dehydroquinate dehydratase; E.C. 4.2.1.10) catalyses the dehydration ...
The in silico design, synthesis, and biological evaluation of ten potent type II dehydroquinase inhi...
Dehydroquinate synthase (DHQS) is a potential target for the development of novel broad-spectrum ant...
The structural changes caused by the substitution of the aromatic moiety in (2<i>S</i>)-2-benzyl-3-d...
The crystal structures of the type II dehydroquinase (DHQase) from Helicobacter pylori in complex wi...
Structural and computational studies to explore the WAT1 binding pocket in the structure-based desig...
SIGLEAvailable from British Library Document Supply Centre-DSC:DXN020422 / BLDSC - British Library D...
The structures of enzymes catalyzing the reactions in central metabolic pathways are generally well...
The recent recrudescence of Mycobacterium tuberculosis infection and the emergence of multidrug-resi...
The enzyme 3-dehydroquinase was purified over 4000-fold to homogeneity from Streptomyces coelicolor....
Structural, biochemical and computational studies to study substrate binding and the role of the con...