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The thermal stability of the Aes acetyl esterase from Escherichia coli has been investigated by means of differential scanning calorimetry and circular dichroism measurements. The calorimetric curves show a denaturation temperature of 68°C for Aes and 61°C for the single point mutant V20D-Aes. The same values are obtained from CD denaturation curves of the two proteins recorded in both the far-UV...
The crystal structure of AFEST, a novel hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus, complexed with a sulphonyl derivative, has been determined and refined to 2.2 Å resolution. This enzyme, which has recently been classified as a member of the hormone- sensitive-lipase (H) group of the esterase/lipase superfamily, presents a canonical α/β hydrolase core, shielded on...
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