Characteristics of an acid active thiamine diphosphatase from beef brain.

That thiamine has a role in nerve conduction as well as synaptic transmission is suggested by the following observations. (1) Thiamine phosphate esters are hydrolyzed and released from nerve membranes during nerve conduction. (2) Ultraviolet radiation of single nerve fibers at the wavelength specific for thiamine destroys the ability of that nerve to conduct an impulse. (3) Thiamine diphosphatase (TDPase) is present on synaptosomes. Previous articles have characterized an alkaline active TDPase in brain; this report characterizes a PH 5 active TDPase and compares it properties to the pH 9 enzyme. Both enzymes require a divalent cation for optimal activity. The pH 5 enzyme is more sensitive to ATP. Myelin fractions of brain have the highest specific activity for the acid TDPase, and the nerve ending particles the highest total activity. No PO4 3-inhibition was observed. Kinetic constants of this enzyme activity are reported.