Bisfunction of propionic acid on purified rat liver beta-ureidopropionase.

Propionic acid and isobutyric acid, which are structural analogues of N-carbamoyl-beta-alanine and N-carbamoyl-beta-aminoisobutyric acid, respectively, acted as an allosteric activator as well as a competitive inhibitor of purified rat liver beta-ureidopropionase. Propionic acid and isobutyric acid had a Ki value of approx. 0.3 mM at pH 7.0. The Hill coefficient for N-carbamoyl-beta-alanine was 2.0, but the cooperatively decreased to 1.0 in the presence of 1 mM propionic acid. The K1/2 value towards N-carbamoyl-beta-alanine was calculated to be 0.17 mM from Hill plots and the Km value was determined to be 0.06 mM from replots of the apparent Km vs propionic acid.