Threonine aldolases-screening, properties and applications in the synthesis of non-proteinogenic beta-hydroxy-alpha-amino acids

Appl Microbiol Biotechnol. 2010 Sep;88(2):409-24. doi: 10.1007/s00253-010-2751-8. Epub 2010 Aug 4.


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 beta-hydroxy-alpha-amino acids. Starting from the achiral precursors glycine and an aldehyde, two new stereogenic centres are formed in this catalytic step. The resulting chiral beta-hydroxy-alpha-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 beta-hydroxy-alpha-amino acids. In this review, screening methods to obtain novel TAs, their biological function, biochemical characterisation and preparative biotransformations with TAs are described.

Publication types

  • Review

MeSH terms

  • Aldehydes / metabolism
  • Amino Acids / biosynthesis
  • Amino Acids / chemical synthesis*
  • Amino Acids / chemistry
  • Glycine / metabolism
  • Glycine Hydroxymethyltransferase / chemistry*
  • Glycine Hydroxymethyltransferase / classification
  • Glycine Hydroxymethyltransferase / isolation & purification*
  • Kinetics
  • Recombinant Proteins / biosynthesis
  • Threonine / metabolism


  • Aldehydes
  • Amino Acids
  • Recombinant Proteins
  • Threonine
  • Glycine Hydroxymethyltransferase
  • Glycine