Studies on bacterial amino-acid decarboxylases

Abstract

1( + )-Arginine decarboxylase has optimum activity at pH 5.25 and Michaelis constant 0.00075M; l( + )-ornithine decarboxylase, pH 555, 0.0039M; 1(+ )-glutamic acid decarboxylase, pH 4.25, 0.027M. 1( + )-Arginine decarboxylase can be resolved into apo-enzyme and codecarboxylase by precipitation with ammoniacal (NH4)2SO4 soln. 1( + )-Ornithine decarboxylase resolves spontaneously on standing into apo-enzyme and codecarboxylase. 1( + )-Glutamic acid decarboxylase was not resolved. The action of common enzyme inhibitors on 6 amino-acid decarboxylases in a cell-free state is descr.