Expression and characterization of Escherichia coli prolidase with organophosphorus compounds Academic Article

abstract

• A relatively high homology between Escherichia coli prolidase and Alteromonas organophosphorous acid anhydrolase suggests that E. coli prolidase may have an activity to degrade toxic organophosphorous compounds. To confirm this suggestion, we cloned and expressed a prolidase gene (pepQ) of E. coli BL21. The recombinant E. coli prolidase that consisted of 443 amino acid residues exhibited activity and stereochemical selectivity against organophosphorous compounds, although its activity was two to three orders of magnitude less than that of the other organophosphorous acid hydrolase isolated from Pseudomonas diminuta. KSBB.

authors

• Raushel, Frank

published proceedings

• BIOTECHNOLOGY AND BIOPROCESS ENGINEERING

author list (cited authors)

• Hong, J. K., Park, M. S., Raushel, F. M., & Khang, Y. H.

complete list of authors

• Hong, JK||Park, MS||Raushel, FM||Khang, YH

publication date

• December 2003

published in

• Biotechnology and Bioprocess Engineering  Journal

keywords

• Chemical Warfare
• Detoxification
• Organophosphorous Compound
• Prolidase

start page

• 126

end page

• 129

volume

• 8

issue

• 2