1996•Protein and Peptide LettersRequires access

Aspartate aminotranferase Thermus aquaticus YT-1. stability from the thermophilic bacterium Functional characterisation and stability

Gennaro Raimo, Mark M. Cassar, Mariorosario Masullo, Vincenzo Bocchini, W.H. Bannister, Joe V. Bannister

Abstract

Abstract: Aspartate aminotranferase from the thermophilic bacterium Thermus aquaticus has been purified to homogeneity. The enzyme is pyridoxal-5-phosphate dependent and is composed of two subunits having an Mr 44000 each. T.aquaticus AspAT shows a pi of 4.5 and is a thermophilic enzyme exhibiting its maximum activity at 80°C in the pH range 7-8. Itis also resistant against denaturation to hea(and several chemical agents.

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Key concepts: Thermus aquaticus, Thermophile, Thermus, Enzyme, Biochemistry, Bacteria, Biology, Chemistry