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The aminotransferase gene family in the model plant  Arabidopsis thaliana  consists of 44 genes. Twenty six of these enzymes are classified as characterized meaning that the reaction(s) that the enzyme catalyzes are documented using experimental means. The remaining 18 enzymes are uncharacterized and are therefore deemed putative. Our laboratory is interested in elucidating the function(s) of the remaining putative aminotransferase enzymes. To this end, we have identified and partially characterized an aminotransferase (TAT) enzyme from Arabidopsis annotated by the locus tag At5g36160. The full-length cDNA was cloned and the purified recombinant enzyme was characterized using  in vitro  and  in vivo  experiments.  In vitro  analysis showed that the enzyme is capable of interconverting L-Tyrosine and 4-hydroxyphenylpyruvate, and L-Phenylalanine and phenylpyruvate.  In vivo  analysis by functional complementation showed that the gene was able to complement an  E. coli  with a background of aminotransferase mutations that confers auxotrophy for L-Tyrosine and L-Phenylalanine.

Identification and Partial Characterization of an L-Tyrosine Aminotransferase (TAT) fromArabidopsis thaliana