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New nitrilase activities.
Nitriles are important intermediates in synthetic chemistry because they are easy to prepare by addition or substitution reactions and they give access to a wide variety of carboxilic acids. However, their chemical hydrolysis requieres harsch experimental conditions and sensitive functions may be damaged. Nitrilases catalyze the hydrolysis of nitrile derivatives into the corresponding carboxylic acids. They are present in various biosynthetic pathways for natural products. In contrast with the chemical hydrolysis conditions, the biocatalytic ones are mild and therefore using the biocatalysts may be a good alternative to the chemical pathway.
Racemization is the transformation of an optically active compound into an equimolar mixture of two enantiomers. In a biocatalytic process, the racemization interest consist in the transformation of the non reactive stereoisomer into the corresponding racemic mixture and therefore the introduction of dynamic equilibrium shift. This is the dynamic kinetic resolution principle.
Unactivated C-H bond oxydation.
Oxydation of unactivated C-H bond is a challenging task for the organic chemist. Our research focuses on the alphaketoglutarate dependant dioxygenases, a non heme iron enzyme family.
Study of the KCE enzyme
Following research on the lysine fermentation pathway, Kce (Keto Cleavage Enzyme, Kreimeyer, A.; Perret, A. et al JBC 2007, 9, 7191) has turned out to be an enzyme of interest which catalyses the reversible conversion of 3-keto-5-aminohexanoate and acetylCoA to (S)-3-aminobutyrylCoA and acetoacetate.
In collaboration with the Pasteur Institute (Paris, France), our results based on a combination of X-ray snapshots and molecular modeling point to an unprecedented mechanism.