AI Article Synopsis
- Phosphotriesterase, an enzyme that breaks down pesticides, was successfully cloned and expressed in E. coli, allowing for further study.
- Replacing zinc ions with cobalt in the enzyme significantly boosted its catalytic activity on various pesticides, enhancing it by 1.4 to 4 times depending on the pesticide.
- Quantum mechanics/molecular mechanics (QM/MM) calculations showed that this increased activity results from a better energy match between the enzyme and substrate, while modifying the enzyme's surface with poly(ethylene glycol) improved its stability and heat resistance.
Article Abstract
Phosphotriesterase, a pesticide-degrading enzyme, from Flavobacterium sp. was cloned and expressed in Escherichia coli. The catalytic zinc ions were replaced by cobalt atoms increasing the catalytic activity of phosphotriesterase on different pesticides. This metal substitution increased the catalytic activity from 1.4 times to 4 times according to the pesticide. In order to explain this catalytic increase, QM/MM calculations were performed. Accordingly, the HOMO energy of the substrate is closer to the LUMO energy of the cobalt-substituted enzyme. The chemical modification of the enzyme surface with poly(ethylene glycol) increased the thermostability and stability against metal chelating agents of both metal phosphotriesterase preparations.
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| http://dx.doi.org/10.1007/s12010-011-9510-x | DOI Listing |
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