despite significant sequence diversity, all known DAH7PS enzymes share a common (beta/alpha)8-barrel core and similar active site architectures formed by conserved residues that support a similar catalytic mechanism. On the basis of sequence and size, DAH7PS enzymes are classified into groups (type Ialpha, type Ibeta and type II). Each group features distinct structural elements appended to the core catalytic barrel that are associated with the allosteric inhibition of the enzymes and different quaternary structure associations. Neisseria meningitidis DAH7PS belongs to the type Ialpha group
shikimate biosynthetic pathway, noncovalent binding to chorismate mutase enhances the mutase activity more than 100fold, 4 enzyme molecules sandwiched between the chorismate mutase dimers reposition the active site of the mutases
3-deoxy-D-arabino-heptulosonate 7-phosphate synthase catalyses the first committed step of the shikimate pathway, which involves the aldol-like condensation of D-erythrose 4-phosphate and phosphoenolpyruvate to form 3-deoxy-D-arabino-heptulosonate 7-phosphate
first enzyme of the shikimate pathway in the biosynthesis of aromatic compounds which is responsible for primary carbohydrate metabolism with the biosynthesis of most aromatic amino acids
first enzyme of the shikimate pathway that link the primary and specialized metabolism derived from aromatic amino acids. Isozyme AroG expression influences the levels of number of primary metabolites, such as shikimic acid and aromatic amino acids, as well as multiple volatile and non-volatile phenylpropanoids specialized metabolites and carotenoids
the enzyme catalyzes the first reaction in the shikimate pathway leading to the biosynthesis of aromatic metabolites including the aromatic acids L-Trp, L-Phe, and L-Tyr. As the entry point, feedback inhibition of DAH7PS by pathway end products is a key mechanism for the control of pathway flux
the enzyme catalyzes the first reaction in the shikimate pathway leading to the biosynthesis of aromatic metabolites including the aromatic acids L-Trp, L-Phe, and L-Tyr. As the entry point, feedback inhibition of DAH7PS by pathway end products is a key mechanism for the control of pathway flux
shikimate biosynthetic pathway, noncovalent binding to chorismate mutase enhances the mutase activity more than 100fold, 4 enzyme molecules sandwiched between the chorismate mutase dimers reposition the active site of the mutases
expression of wild-type enzyme and phenylalanine-feedback insensitive mutant L175Q in Arabidopsis thaliana. Transgenic plants have comparable phenotypes and are fully fertile. The levels of shikimate, prephenate and Phe are higher in the different lines expressing the mutant enzyme than in the lines expressing the natural feedback-sensitive bacterial enzyme, and the control plants. Results imply that the bacterial enzyme is active in the transgenic plants and, similar to its operation in bacteria, the feedback insensitivity trait of the mutant enzyme is fundamental for enhancement of the flow of primary carbon metabolites via the shikimate pathway into the production of aromatic amino acids also in the plant
3-deoxy-D-arabino-heptulosonate 7-phosphate synthase catalyses the aldol-like condensation of D-erythrose 4-phosphate and phosphoenolpyruvate to form 3-deoxy-D-arabino-heptulosonate 7-phosphate. Entry into the pathway is controlled by the allosteric regulation of enzyme DAH7PS by the pathway end products Phe, Tyr and Trp, or other intermediates of the pathway
allosteric response arising from changes in protein motion rather than conformation, and suggest ligands that modulate protein dynamics may be effective inhibitors of this enzyme. The nature of the extra barrel extensions is directly implicated in the sensitivity of the DAH7PS enzymes to allosteric control
allosteric response arising from changes in protein motion rather than conformation, and suggest ligands that modulate protein dynamics may be effective inhibitors of this enzyme. The nature of the extra barrel extensions is directly implicated in the sensitivity of the DAH7PS enzymes to allosteric control
allosteric response arising from changes in protein motion rather than conformation, and suggest ligands that modulate protein dynamics may be effective inhibitors of this enzyme. The nature of the extra barrel extensions is directly implicated in the sensitivity of the DAH7PS enzymes to allosteric control