Amino acid metabolism in acetic acid bacteria. III. Purification and some properties of L-leucine-pyruvate transaminase from Acetobacter suboxydans.

Abstract

An enzyme, tentatively named l-leucine-pyruvate transaminase, was purified homogeneously by the criteria of ultracentrifugation and electrophoresis on a cellulose acetate membrane from Acetobacter suboxydans (Gluconobacter suboxydans IFO 3172). The molecular weight was about 70,000 and one mole of pyridoxal 5′-phosphate was bound per mole of the enzyme as coenzyme. The amino donor specificity was extremely broad and the optimum pH was 5.0. The enzyme exhibit absorption maxima at 280 nm and 332 nm.