A Second Form of Phenylalanine Ammonia-Lyase from Leaf Mustard

초록

Phenylalanine ammonia-lyase (PAL, EC 4.3.1.5) catalyzes the elimination of ammonium ion from L-phenylalanine in a variety of plants and fungal species. PAL was previously purified and characterized from leaf mustard in our laboratory. In the present study, we purified a second phenylalanine ammonialyase (PAL II) from leaf mustard by a combination of ion exchange chromatography and gel filtration. PAL I and PAL II migrate at a different rate on native polyacrylamide gel electrophoresis. It consists of four subunits, each having the molecular mass of about 37,000 Da. Its isoelectric point and K<inf>M</inf> value for L-phenylalanine were found to be 5.4 and 3.8 ×10 -5 M, respectively. The purified enzyme has an optimum pH and temperature of 8 and 45°C, respectively. It is activated about 2-fold by caffeic acid (1 mM), whereas it is inhibited to 15% by Zn2+ (1 mM). However, the physiological role of PAL II remains unknown.

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