Sulfolobal phosphotriesterase-like (PLL) lactonases activity having enhanced properties and the uses thereof
AssigneesCentre National De La Recherche Scientifique, Universite D'Aix-Marseille
InventorsEric Chabriere, Mikael Elias, Julien Hiblot, Didier Raoult
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Abstract
Mutated hyperthermophilic PTE having a lactonase activity derived from a hyperthermophilic phosphotriesterase corresponding to the consensus sequence of SEQ ID NO: 1, the mutated PTE including the at least one mutation chosen amongst 53 putative positions and the mutated PTE having enhanced properties. Also provided are compositions including the mutated hyperthermophilic PTE and the uses thereof, notably as bioscavenger of organophosphate compounds or as quorum quencher of the bacteria using lactones to communicate.
Claims22
A mutated hyperthermophilic phosphotriesterase, said mutated hyperthermophilic phosphotriesterase has an increased lactonase catalytic activity in comparison of the lactonase activity of a non-mutated hyperthermophilic phosphotriesterase, wherein the non-mutated hyperthermophilic phosphotriesterase is a wild-type phosphotriesterase corresponding to the consensus sequence of SEQ ID NO:1, wherein the amino acid W in position 265 is substituted by an amino acid selected from the group consisting of the amino acids isoleucine I, valine V, threonine T and alanine A within the mutated hyperthermophilic phosphotriesterase.
A mutated hyperthermophilic phosphotriesterase, said mutated hyperthermophilic phosphotriesterase has an increased lactonase catalytic activity in comparison of the lactonase activity of a non-mutated hyperthermophilic phosphotriesterase, wherein the non-mutated hyperthermophilic phosphotriesterase is a wild-type phosphotriesterase corresponding to the consensus sequence of SEQ ID NO:1, wherein the amino acid W in position 265 is the single substitution within the mutated hyperthermophilic phosphotriesterase.
Dependencies are inferred from the claim text.