Purification and Characterization of L-Leucine-α-ketoglutarate Transaminase from Acetobacter suboxydans

Abstract

L-Leucine-α-ketoglutarate (α-KGA) transaminase from Acetobacter suboxydans was purified to the state of homogeneity by the criteria of ultracentrifugation and electrophoresis on a cellulose acetate membrane. The molecular weight was about 80, 000 and one mole of pyridoxal 5'-phosphate was bound per mole of enzyme as a coenzyme. The enzyme exhibited absorption maxima at 280, 337 and 414 nm.
The branched-chain amino acids and αa-KGA were specific as amino donors and an acceptor. L-Leucine-α-KGA transaminase is suggested to correspond to the enzyme so-called Transaminase B.