Yeast glutamate-cr-ketoadipate transaminase activity exhibited differences in differential heat inactivation, pH dependence, response to pyridoxal phosphate, ammonium sulfate fractionation, diethylaminoethyl cellulose chromatography, and mutational independence from other known transaminases. Both yeast glutamate-ol-ketoadipate transaminase and glutamate-pyruvate transaminase were found to be p...