ENZYMATIC BREAKDOWN OF THREONINE BY THREONINE ALDOLASE

Abstract

The enzyme which forms glycine and acetalde- hyde from threonine was partially purified and its properties studied. Optimum activity is at pH 7.5-7.7 and the enzyme is unstable below pH 5. The optimum temperature is about 50[degree]C. The enzyme is about 25 times more active for L-allothreonine than for L-threonine. It does not attack corresponding D-amino acids nor serine. Equivalent amounts of acetaldehyde and gly-cine are formed from allothreonine and the enzymatic break-down was found to be irreversible.