An OPAA enzyme mutant with increased catalytic efficiency on the nerve agents sarin, soman, and GP. Academic Article

abstract

• The wild-type OPAA enzyme has relatively high levels of catalytic activity against several organophosphate G-type nerve agents. A series of mutants containing replacement amino acids at the OPAA Y212, V342, and I215 sites showed several fold enhanced catalytic efficiency on sarin, soman, and GP. One mutant, Y212F/V342L, showed enhanced stereospecificity on sarin and that enzyme along with a phosphotriesterase mutant, GWT, which had the opposite stereospecificity, were used to generate enriched preparations of each sarin enantiomer. Inhibition of acetylcholinesterase by the respective enantioenriched sarin solutions subsequently provided identification of the sarin enantiomers as separated by normal phase enantioselective liquid chromatography coupled with atmospheric pressure chemical ionization-mass spectrometry.

authors

• Raushel, Frank

published proceedings

• Enzyme Microb Technol

altmetric score

• 0.75

author list (cited authors)

• Bae, S. Y., Myslinski, J. M., McMahon, L. R., Height, J. J., Bigley, A. N., Raushel, F. M., & Harvey, S. P.

citation count

• 28

complete list of authors

• Bae, Sue Y||Myslinski, James M||McMahon, Leslie R||Height, Jude J||Bigley, Andrew N||Raushel, Frank M||Harvey, Steven P

publication date

• May 2018

publisher

• Elsevier  Publisher

published in

• Enzyme and Microbial Technology  Journal

keywords

• Amino Acid Sequence
• Amino Acid Substitution
• Aryldialkylphosphatase
• Biocatalysis
• Gp
• Kinetics
• Lc-apci-ms
• Mutagenesis
• Mutagenesis, Site-Directed
• Nerve Agents
• Opaa
• Organophosphorus Compounds
• Recombinant Proteins
• Sarin
• Soman
• Stereoisomerism
• Substrate Specificity

Digital Object Identifier (DOI)

• 10.1016/j.enzmictec.2017.11.001

start page

• 65

end page

• 71

volume

• 112

URL

• http://dx.doi.org/10.1016/j.enzmictec.2017.11.001