Identification of a plant gene encoding glutamate/aspartate-prephenate aminotransferase: the last homeless enzyme of aromatic amino acids biosynthesis

FEBS Lett. 2010 Oct 22;584(20):4357-60. doi: 10.1016/j.febslet.2010.09.037. Epub 2010 Sep 29.

Abstract

In all organisms synthesising phenylalanine and/or tyrosine via arogenate, a prephenate aminotransferase is required for the transamination of prephenate into arogenate. The identity of the gene encoding this enzyme in the organisms where this activity occurs is still unknown. Glutamate/aspartate-prephenate aminotransferase (PAT) is thus the last homeless enzyme in the aromatic amino acids pathway. We report on the purification, mass spectrometry identification and biochemical characterization of Arabidopsis thaliana prephenate aminotransferase. Our data revealed that this activity is housed by the prokaryotic-type plastidic aspartate aminotransferase (At2g22250). This represents the first identification of a gene encoding PAT.

MeSH terms

  • Amino Acids, Aromatic / metabolism*
  • Arabidopsis / cytology
  • Arabidopsis / enzymology
  • Arabidopsis / genetics
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism*
  • Aspartate Aminotransferases / genetics
  • Aspartate Aminotransferases / metabolism*
  • Cells, Cultured
  • Electrophoresis, Polyacrylamide Gel
  • Glutamic Acid / metabolism
  • Kinetics
  • Mass Spectrometry
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Transaminases / genetics
  • Transaminases / metabolism*

Substances

  • Amino Acids, Aromatic
  • Arabidopsis Proteins
  • Recombinant Proteins
  • Glutamic Acid
  • Transaminases
  • prephenate aminotransferase
  • Aspartate Aminotransferases