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PLANT PHYSIOLOGY , Vol 113, Issue 1 175-179, Copyright © 1997 by American Society of Plant Biologists
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BIOCHEMISTRY AND ENZYMOLOGY |
Maize Phenylalanine Ammonia-Lyase Has Tyrosine Ammonia-Lyase Activity
J. Rosler, F. Krekel, N. Amrhein and J. Schmid
Institute of Plant Sciences, Swiss Federal Institute of Technology, Universitatstrasse 2, CH-8092 Zurich, Switzerland
A full-length cDNA encoding phenylalanine ammonia-lyase (PAL) from Zea mays
L. was isolated and the coding region was expressed in Escherichia coli as
a C-terminal fusion to glutathione S-transferase. After purification by
glutathione-Sepharose chromatography, the glutathione S-transferase moiety
was cleaved off and the resulting PAL enzyme analyzed. In contrast to PAL
from dicots, this maize PAL isozyme catalyzed the deamination of both
L-phenylalanine (PAL activity) and L-tyrosine (tyrosine ammonialyase
activity). These results provide unequivocal proof that PAL and tyrosine
ammonia-lyase activities reside in the same polypeptide. In spite of large
differences in the Michaelis constant and turnover number of the two
activities, their catalytic efficiencies are very similar. Also, both
activities have the same pH and temperature optima. These results imply
that maize can produce p-coumaric acid from both phenylalanine and
tyrosine.
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