The regulation of 3-deoxy-D-arabino-heptulosonate 7 phosphate synthase from Mycobacterium tuberculosis.

by Nicola Jean Blackmore

Institution: University of Canterbury
Department: Chemistry
Year: 2015
Keywords: DAH7PS; allostery; enzymes; regulation; chromate mutate; shikimate pathway
Record ID: 1314371
Full text PDF: http://hdl.handle.net/10092/10242


Allosteric regulation of important enzymes is a mechanism frequently employed by organisms to exert control over their metabolism. The shikimate pathway is ultimately responsible for the biosynthesis of the aromatic amino acids in plants, microorganisms and apicomplexans. Two enzymes of the pathway, 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAH7PS) and chorismate mutase (CM) are located at critical positions along the aromatic amino acid biosynthetic pathway and are often tightly feedback regulated in order to control the flux of metabolites through the pathway. This research presents studies on the allosteric function of these two enzymes. These studies emphasise the complexity of the intersecting network of allosteric response, which alters the catalytic activity of each enzyme in response to metabolic demand for the aromatic amino acids.