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Conversion of L- and D-Phenylalanine to Phenylacetate via Phenylpyruvate in Sorghum Leaf Extracts ¹

^a Department of Biology, Reed College, Portland, Oregon 97202

The incorporation of DL-[¹⁴C]phenylalanine into phenylacetate reported previously in leaf enzyme preparations has been found to be catalyzed by two separate enzyme activities leading to phenylpyruvate, one using the L-, the other the D-isomer. Since both reactions occur anaerobically and are increased by the addition of pyridoxal phosphate and -ketoglutarate, two transaminase (aminotransferase) activities appear to be involved. The activities of the L- and D-dependent forms are approximately equal in a crude particulate fraction, but range from 1:1 to 3:1 in a soluble supernatant fraction. Nonisotopic as well as isotopic assays to separate D- and L-activities are described.