Stereochemistry and mechanism of a microbial phenylalanine aminomutase

J Am Chem Soc. 2011 Jun 8;133(22):8531-3. doi: 10.1021/ja2030728. Epub 2011 May 11.


The stereochemistry of a phenylalanine aminomutase (PAM) on the andrimid biosynthetic pathway in Pantoea agglomerans (Pa) is reported. PaPAM is a member of the 4-methylidene-1H-imidazol-5(4H)-one (MIO)-dependent family of catalysts and isomerizes (2S)-α-phenylalanine to (3S)-β-phenylalanine, which is the enantiomer of the product made by the mechanistically similar aminomutase TcPAM from Taxus plants. The NH(2) and pro-(3S) hydrogen groups at C(α) and C(β), respectively, of the substrate are removed and interchanged completely intramolecularly with inversion of configuration at the migration centers to form β-phenylalanine. This is a contrast to the retention of configuration mechanism followed by TcPAM.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Catalysis
  • Molecular Structure
  • Pantoea / enzymology*
  • Phenylalanine / chemistry*
  • Phenylalanine Ammonia-Lyase / chemistry*
  • Phenylalanine Ammonia-Lyase / metabolism
  • Stereoisomerism


  • Phenylalanine
  • Phenylalanine Ammonia-Lyase