An OPAA enzyme mutant with increased catalytic efficiency on the nerve agents sarin, soman, and GP
| Autor: | J.J. Height, Andrew N. Bigley, Leslie R. Mcmahon, James M. Myslinski, Steven P. Harvey, Sue Y. Bae, Frank M. Raushel |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Sarin Stereochemistry Soman Bioengineering Applied Microbiology and Biotechnology Biochemistry Substrate Specificity 03 medical and health sciences chemistry.chemical_compound Organophosphorus Compounds Stereospecificity medicine Amino Acid Sequence Nerve agent chemistry.chemical_classification 030102 biochemistry & molecular biology Aryldialkylphosphatase Organophosphate Stereoisomerism Acetylcholinesterase Recombinant Proteins Kinetics 030104 developmental biology Enzyme Amino Acid Substitution chemistry Biocatalysis Mutagenesis Site-Directed Enantiomer Nerve Agents Biotechnology medicine.drug |
| Zdroj: | Enzyme and Microbial Technology. 112:65-71 |
| ISSN: | 0141-0229 |
| DOI: | 10.1016/j.enzmictec.2017.11.001 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect