In this work, the variant 10-2-C3 of the phosphotriesterase from
Brevundimonas diminuta was further developed with regard to its catalytic activity and stability in order to be used later as an antidote for intoxication with organophosphorus compounds. To this end, the oxidative sensitivity of the enzyme was reduced and the structure of a promising variant was elucidated by X-ray crystallography, among others. The results show that the investigated variant, despite a so far erroneous structural model, is already well-optimized for the hydrolysis of organophosphorus compounds.
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In this work, the variant 10-2-C3 of the phosphotriesterase from
Brevundimonas diminuta was further developed with regard to its catalytic activity and stability in order to be used later as an antidote for intoxication with organophosphorus compounds. To this end, the oxidative sensitivity of the enzyme was reduced and the structure of a promising variant was elucidated by X-ray crystallography, among others. The results show that the investigated variant, despite a so far erroneous structural...
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