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

Purification, crystallization and preliminary crystallographic analysis of DehIVa, a dehalogenase from Burkholderia cepacia MBA4

Buy Article:

$52.00 + tax (Refund Policy)

DehIVa is one of two dehalogenases produced by the soil‐ and water‐borne bacterium Burkholderia cepacia MBA4. It acts to break down short‐chain halogenated aliphatic acids through a nucleophilic attack and subsequent hydrolysis of an enzyme–substrate intermediate to remove the halide ions from l‐enantiomers substituted at the C2 position (‐2‐monochloropropionic acid). Dehalogenases are an important group of enzymes that are responsible for breaking down a diverse range of halogenated environmental pollutants. The dhlIVa gene coding for DehIVa was expressed in Escherichia coli and the protein was purified and crystallized using the hanging‐drop method. Crystals grown in PEG 4000 and ammonium sulfate diffracted to 3.1 Å. The crystals had a primitive hexagonal unit cell, with unit‐cell parameters a = b = 104.2, c = 135.8 Å, α = β = 90, γ = 120°. Determining this structure will provide valuable insights into the characterization of the catalytic mechanisms of this group of enzymes.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: Burkholderia cepacia MBA4; DehIVa; dehalogenases; halogenated organic acids

Document Type: Research Article

Publication date: March 1, 2005

  • 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