Abstract
Purified cauliflower transaminase is stimulated by a maximum of threefold when incubated with pyridoxal 5-phosphate or pyridoxamine 5-phosphate. The enzyme is inhibited by isoiazid, and this inhibition is reversed by pryi-doxal 5-phosphate. Determinations of several kinetic constants are reported; these constants provide evidence which supports a mechanism of enzyme action involving a binary complex.