Skip to main content
padlock icon - secure page this page is secure

Expression, purification, crystallization and preliminary X‐ray diffraction analysis of dihydrodipicolinate synthase from Bacillus anthracis in the presence of pyruvate

Buy Article:

$52.00 + tax (Refund Policy)

Dihydrodipicolinate synthase (DHDPS) catalyses the first committed step in the lysine‐biosynthesis pathway in bacteria, plants and some fungi. In this study, the expression of DHDPS from Bacillus anthracis (Ba‐DHDPS) and the purification of the recombinant enzyme in the absence and presence of the substrate pyruvate are described. It is shown that DHDPS from B. anthracis purified in the presence of pyruvate yields greater amounts of recombinant enzyme with more than 20‐fold greater specific activity compared with the enzyme purified in the absence of substrate. It was therefore sought to crystallize Ba‐DHDPS in the presence of the substrate. Pyruvate was soaked into crystals of Ba‐DHDPS prepared in 0.2 M sodium fluoride, 20%(w/v) PEG 3350 and 0.1 M bis‐tris propane pH 8.0. Preliminary X‐ray diffraction data of the recombinant enzyme soaked with pyruvate at a resolution of 2.15 Å are presented. The pending crystal structure of the pyruvate‐bound form of Ba‐DHDPS will provide insight into the function and stability of this essential bacterial enzyme.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: anthrax; antibiotic resistance; antibiotics; dihydrodipicolinate synthase; drug discovery; lysine biosynthesis

Document Type: Research Article

Publication date: February 1, 2009

  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more