Phenylalanine ammonia lyase (PAL), a key enzyme of the phenylpropanoid pathway, catalyzes the conversion of phenylalanine (Phe) to trans-cinnamic acid and in some instances tyrosine (Tyr) to para-hydroxycinnamic acid. PAL from the yeast Trichosporon cutaneum (Tc) was selected as a model to further investigate the tyrosine ammonia lyase activity of this family of enzymes. TcPAL exhibited highest Phe:Tyr activities (1.6 � 0.3 : 0.4 � 0.1 �mol/h g wet weight) when induced with Tyr (2 mM). The enzyme displayed Michaelis Menten kinetics with Phe (Km 5.0 � 0.7 mM) but allosteric kinetics with Tyr (K' 1.7 � 0.8 mM, Hill coefficient 1.8 � 0.2). Highest purification fold and yields of the enzyme were obtained from anion exchange chromatography. The PAL gene was cloned into the pET30a vector, under control of the T7 lac promotor. Five amino acid residues not previously reported were detected, namely Glu74, Ala274, Val298, Pro322 and Lys486.

Investigation of the phenylalanine ammonia lyase activity   in the yeast <i>Trichosporon cutaneum</i>

243rd National Meeting (2012)

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Investigation of the phenylalanine ammonia lyase activity in the yeast Trichosporon cutaneum