The mitochondrial branched-chain aminotransferase (AtBCAT-1) is capable to initiate degradation of leucine, isoleucine and valine in almost all tissues in Arabidopsis thaliana.

Plants are capable to de novo synthesize the essential amino acids leucine, isoleucine and valine. Studies in recent years, however, also revealed that plants have the potential to degrade leucine or may be all of the branched-chain amino acids. One of the enzymes participating in both biosynthesis and degradation is the branched-chain aminotransferase, which is in Arabidopsis thaliana encoded by a small gene family with six transcribed members. We have now studied the steady state mRNA levels by quantitative RT-PCR and promoter activities of these genes with promoter::glucuronidase reporter gene constructs in transgenic plants. The gene encoding the mitochondrial isoenzyme (Atbcat-1) is expressed in all tissues with predominant transcription in seedlings and leaves. Surprisingly the plastid located proteins (AtBCAT-2, -3 and -5) are expressed at rather low levels with only Atbcat-3 transcribed in all tissues. The most likely cytoplasmic-located AtBCAT-4 and AtBCAT-6 are mainly expressed in tissues associated with transport function and in meristematic tissues, respectively. A detailed characterization of the enzyme activity and substrate specificity of the mitochondrial AtBCAT-1 enzyme revealed the potential of this enzyme to initiate degradation of all branched-chain amino acids. In addition alpha-aminobutyrate and alpha-ketobutyrate as well as methionine and alpha-ketomethylthiobutyrate are identified as substrates. This suggests that AtBCAT-1 and potentially other members of this protein family may influence methionine levels and may play an important role in the metabolism of the nonprotein amino acid alpha-aminobutyrate. The consequences of these substrate specificities for bioplastic production and methionine homeostasis are discussed.