Abstract
Several properties of the L-glutamic acid decarboxylase in the cell-free extract of bacteria are described.
a) The optimum pH of the L-glutamic acid decarboxylase is 5.0.
b) The reaction velocity of the enzyme in different concentrations of the substrate (L-glutamic acid) is estimated, and the Km value of the enzyme calculated by the Lineweaver-Burk method is 3.85×10-3M.
c) Hydroxylamine and semicarbazide which are known as aldehyde reagents, inhibit the activity of this enzyme completely in a concentration of 6×10-4, 1.6×10-3M/l. respectively. It suggests a presence of CO group in the enzyme as an active center.
d) The active enzyme is precipitated without an activity loss by changing the hydregen concentration of the cell-free extract with use of acetic acid.
