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Two new thermophilic branched chain amino acid transaminases have been identified within the genomes of different hyper-thermophilic archaea,  Geoglobus acetivorans , and  Archaeoglobus fulgidus . These enzymes belong to the class IV of transaminases as defined by their structural fold. The enzymes have been cloned and over-expressed in  Escherichia coli  and the recombinant enzymes have been characterized both biochemically and structurally. Both enzymes showed high thermostability with optimal temperature for activity at 80 and 85°C, respectively. They retain good activity after exposure to 50% of the organic solvents, ethanol, methanol, DMSO and acetonitrile. The enzymes show a low activity to ( R )-methylbenzylamine but no activity to ( S )-methylbenzylamine. Both enzymes have been crystallized and their structures solved in the internal aldimine form, to 1.9 Å resolution for the  Geoglobus  enzyme and 2.0 Å for the  Archaeoglobus  enzyme. Also the  Geoglobus  enzyme structure has been determined in complex with the amino acceptor α-ketoglutarate and the  Archaeoglobus  enzyme in complex with the inhibitor gabaculine. These two complexes have helped to determine the conformation of the enzymes during enzymatic turnover and have increased understanding of their substrate specificity. A comparison has been made with another ( R ) selective class IV transaminase from the fungus  Nectria haematococca  which was previously studied in complex with gabaculine. The subtle structural differences between these enzymes has provided insight regarding their different substrate specificities.

frontiers in bioengineering and biotechnology

Thermostable Branched-Chain Amino Acid Transaminases From the Archaea Geoglobus acetivorans and Archaeoglobus fulgidus: Biochemical and Structural Characterization