Plant Physiol. Illumina
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Plant Physiology 97:1494-1500 (1991)
© 1991 American Society of Plant Biologists

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Metabolism and Enzymology

Phenylalanine Ammonia-Lyase from Tomato Cell Cultures Inoculated with Verticillium albo-atrum 1

Mark A. Bernards2 and Brian E. Ellis

Department of Plant Science, University of British Columbia, 2357 Main Mall, Vancouver, British Columbia, Canada, V6T 2A2

Tomato (Lycopersicon esculentum Mill.) cell suspension cultures accumulated wall-bound phenolic materials in response to inoculation with Verticillium albo-atrum Reinke et Berth. in a fashion analogous to that observed in whole plants. Both monomeric and polymeric materials were recovered. Deposition of phenolics into the cell walls of inoculated tomato cell cultures was inhibited by the phenylalanine ammonia-lyase (PAL) inhibitor, 2-amino-2-indanephosphate. Tomato PAL activity was induced over 12-fold by fungal inoculation, with a concomitant increase in the corresponding mRNA. The enzyme was purified >3400-fold, to apparent homogeneity, by anion-exchange chromatography, chromatofocusing, and gel filtration. The holoenzyme had a molecular mass of 280 to 320 kilodaltons, comprising 74-kilodalton subunits, and displayed an isoelectric point of 5.6 to 5.7. Induced PAL displayed apparent Michaelis-Menten kinetics (Km = 116 micromolar) and was not appreciably inhibited by its product cinnamic acid. Chromatographic analysis did not reveal multiple forms of the enzyme in either inoculated or uninoculated cultures.

2 Present address: Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340.

1 Supported in part by the Natural Sciences and Engineering Research Council of Canada.




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A. Chang, M.-H. Lim, S.-W. Lee, E. J. Robb, and R. N. Nazar
Tomato Phenylalanine Ammonia-Lyase Gene Family, Highly Redundant but Strongly Underutilized
J. Biol. Chem., November 28, 2008; 283(48): 33591 - 33601.
[Abstract] [Full Text] [PDF]


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Copyright © 1991 by the American Society of Plant Biologists