Metabolism of Aromatic Amino Acid in Microorganisms

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Abstract
Phenylalanine ammonia -lyase, which catalyzes the conversion of L-phenylalanine to trans-cinnamic acid and ammonia, has been partially purified from the cells of Rhodotorula. Some of the properties of this phenylalanine ammonia-lyase were investigated. The enzyme was stable in phosphate buffer of pH over the range of 6.0 to 7.0. On heating, the enzyme was stable up to 50[degree]C, but above 60[degree]C, it was destroyed. The enzyme activity was strongly inhibited by p-chloromerucuri-benzoate at 10-5 M and almost recovered by the addition of glutathione or mercaptoethanol at 10-3 M. The present enzyme preparation of Rhodotorula also catalyzed and deamination of L-tyrosine to trans-p-coumaric acid. trans-p-Coumaric acid was isolated from the reaction mixture and identified by its absorption spectra. The rates of deamination showed optima at pH 9.0 and 9.5 for L-phenylalanine and L-tyrosine, respectively.

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