Transaminases for the synthesis of enantiopure beta-amino acids

  • Rudat J
  • Brucher B
  • Syldatk C
  • 127

    Readers

    Mendeley users who have this article in their library.
  • 32

    Citations

    Citations of this article.

Abstract

Optically pure β-amino acids constitute interesting building blocks for peptidomimetics and a great variety of pharmaceutically important compounds. Their efficient synthesis still poses a major challenge. Transaminases (also known as aminotransferases) possess a great potential for the synthesis of optically pure β-amino acids. These pyridoxal 5'-dependent enzymes catalyze the transfer of an amino group from a donor substrate to an acceptor, thus enabling the synthesis of a wide variety of chiral amines and amino acids. Transaminases can be applied either for the kinetic resolution of racemic compounds or the asymmetric synthesis starting from a prochiral substrate. This review gives an overview over microbial transaminases with activity towards β-amino acids and their substrate spectra. It also outlines current strategies for the screening of new biocatalysts. Particular emphasis is placed on activity assays which are applicable to high-throughput screening.

Author-supplied keywords

  • beta-amino acid
  • biocatalysis
  • high-throughput screening
  • transaminase

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Get full text

Authors

  • Jens Rudat

  • Birgit R. Brucher

  • Christoph Syldatk

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free