Expression and Characterization of Escherichia coli Prolidase with Organophosphorus Compounds

  • Hong, Jin-Kyu (EM Industrial Corporation) ;
  • Park, Min-Sun (Department of chemistry, Texas A&M University) ;
  • Frank M. Raushel (Department of chemistry, Texas A&M University) ;
  • Khang, Yong-Ho (Department of Applied Microbiology, Yeungnam University)
  • Published : 2003.04.01

Abstract

A relatively high homology between Escherichia coli prolidase and Alteromonas organophosphorous acid anhydrolase suggests that E. coli prolidase may have an activity to d egrade toxic organophosphorous compounds. To confirm this suggestion, we cloned and expressed a prolidase gene (pepQ) of E. coliBL2l. The recombinant E. coli prolidase that consisted of 443 amino acid residues exhibited activity and stereochemical selectivity against organopho sphorous compounds, although its activity was two to three orders of magnitude less than that of the other organophosphorous acid hydrolase isolated from Pseudomonas diminuta.

Keywords

References

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