Applied Microbiology and Biotechnology

, Volume 88, Issue 2, pp 409–424

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


DOI: 10.1007/s00253-010-2751-8

Cite this article as:
Dückers, N., Baer, K., Simon, S. et al. Appl Microbiol Biotechnol (2010) 88: 409. doi:10.1007/s00253-010-2751-8


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 

Copyright information

© Springer-Verlag 2010

Authors and Affiliations

  1. 1.evocatal GmbHDüsseldorfGermany
  2. 2.Department of Chemistry and PharmacyUniversity of Erlangen-NurembergErlangenGermany
  3. 3.Institute of Molecular Enzyme TechnologyHeinrich-Heine-University of Düsseldorf, Research Centre JülichJülichGermany

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