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SUMMARY:Exploring the evolutionary relationships and the reaction chemistr
 y in a family of crucial biosynthetic aldolases -  Professor Emily J Parke
 r\, University of Canterbury - Christchurch\, New Zealand
DTSTART:20100524T160000Z
DTEND:20100524T170000Z
UID:TALK24749@talks.cam.ac.uk
CONTACT:Jane Snaith
DESCRIPTION:3-Deoxy-d-manno-octulosonate 8-phosphate (KDO8P) synthase and 
 3-deoxy-d-arabino-heptulosonate 7-phosphate (DAH7P) synthase are two enzym
 es that catalyse related reactions in two distinct biosynthetic pathways. 
  KDO8P synthase is responsible for the formation of an essential component
  of the lipopolysaccharide in Gram-negative bacteria.  DAH7P synthase cata
 lyses the first step of the shikimate pathway to aromatic amino acids.  Bo
 th enzymes have been identified as targets for drug design. \nWe have used
  a combination of structural studies\, substrate analogues and site-direct
 ed mutagenesis to probe small but significant differences in the active si
 tes of these two enzymes.  These studies have illuminated important mechan
 istic differences and have clarified the evolutionary relationship between
  these two enzymes.  In addition\, we have shown that the activity of the 
 M. tuberculosis DAH7P synthase is regulated synergistically by a combinati
 on of two aromatic amino acids\, demonstrating an unusual mechanism for th
 e regulation of aromatic metabolism.\n
LOCATION:Unilever Lecture Theatre\,  Department of Chemistry
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