Applied Microbiology and Biotechnology

, Volume 88, Issue 2, pp 409-424

First online:

Threonine aldolases—screening, properties and applications in the synthesis of non-proteinogenic β-hydroxy-α-amino acids

  • Nina DückersAffiliated withevocatal GmbH
  • , Katrin BaerAffiliated withDepartment of Chemistry and Pharmacy, University of Erlangen-Nuremberg
  • , Sabine SimonAffiliated withDepartment of Chemistry and Pharmacy, University of Erlangen-Nuremberg
  • , Harald GrögerAffiliated withDepartment of Chemistry and Pharmacy, University of Erlangen-Nuremberg Email author 
  • , Werner HummelAffiliated withInstitute of Molecular Enzyme Technology, Heinrich-Heine-University of Düsseldorf, Research Centre Jülich Email author 

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Threonine aldolases (TAs) constitute a powerful tool for catalyzing carbon–carbon bond formations in synthetic organic chemistry, thus enabling an enantio- and diastereoselective synthesis of β-hydroxy-α-amino acids. Starting from the achiral precursors glycine and an aldehyde, two new stereogenic centres are formed in this catalytic step. The resulting chiral β-hydroxy-α-amino acid products are important precursors for pharmaceuticals such as thiamphenicol, a l-threo-phenylserine derivative or l-threo-3,4-dihydroxyphenylserine. TAs are pyridoxal-5-phosphate-dependent enzymes, which, in nature, catalyze the cleavage of l-threonine or l-allo-threonine to glycine and acetaldehyde in a glycine biosynthetic pathway. TAs from a broad number of species of bacteria and fungi have been isolated and characterised as biocatalysts for the synthesis of β-hydroxy-α-amino acids. In this review, screening methods to obtain novel TAs, their biological function, biochemical characterisation and preparative biotransformations with TAs are described.


Threonine aldolases Carbon–carbon bond formation Racemic resolution Asymmetric synthesis Phenylserine Review