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Synthesis of beta-hydroxy-alpha-amino acids with a reengineered alanine racemase.
Journal article

Synthesis of beta-hydroxy-alpha-amino acids with a reengineered alanine racemase.

  • Fesko K Laboratory of Organic Chemistry, ETH Zürich, Hönggerberg HCI F339, 8093 Zurich, Switzerland.
  • Giger L
  • Hilvert D
  • 2008-09-02
Published in:
  • Bioorganic & medicinal chemistry letters. - 2008
Alanine
Alanine Racemase
Aldehydes
Amino Acids
Bacteria
Catalysis
Combinatorial Chemistry Techniques
Glycine
Glycine Hydroxymethyltransferase
Molecular Structure
Protein Engineering
Pyridoxal Phosphate
Stereoisomerism
English The Y265A mutant of alanine racemase (alrY265A) was evaluated as a catalyst for the synthesis of beta-hydroxy-alpha-amino acids. It promotes the PLP-dependent aldol condensation of glycine with a range of aromatic aldehydes. The desired products were obtained with complete stereocontrol at C(alpha) (ee>99%, D) and moderate to high selectivity at C(beta) (up to 97% de). The designed enzyme is thus similar to natural d-threonine aldolases in its substrate specificity and stereoselectivity. Moreover, its ability to utilize alanine as an alternative donor suggests an expanded scope of potential utility for the production of biologically active compounds.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://folia.unifr.ch/global/documents/123672
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