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Mariana L. Gutierrez, Xavier Garrabou, Eleonora Agosta, Stefano Servi, Teodor Parella, Jesús Joglar and Pere Clapés Serine Hydroxymethyl Transferase from Streptococcus thermophilus and L-Threonine Aldolase from Escherichia coli as Stereocomplementary Biocatalysts for the Synthesis of β-Hydroxy-α,ω-diamino Acid Derivatives Chemistry - A European Journal 14

Version of Record online: 2 APR 2008 | DOI: 10.1002/chem.200800031

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Glycine-dependent aldolases: A hydroxymethyl transferase from S. thermophilus (SHMT) at 4 °C and L-threonine aldolase from E. coli at 25 °C gave L-erythro and L-threo aldol adducts, respectively (see scheme; Cbz=benzyloxycarbonyl). SHMT turned out to be among the most stereoselective glycine aldolases. Both enzymes were applied to the synthesis of 2,4-diamino-3-hydroxy acid derivatives, which are polyfunctional intermediates for the preparation of bioactive molecules.

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