+ Site Statistics
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity

Plant physiology 113(1): 175-179
Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity
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.

Accession: 002889105

PMID: 9008393

DOI: 10.1104/pp.113.1.175

Download PDF Full Text: Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity

Related references

Activity of phenylalanine ammonia-lyase, tyrosine ammonia-lyase, and cinnamyl alcohol dehydrogenase in the maize stalk. Crop Science 33(6): 1264-1268, 1993

Phenylalanine ammonia lyase tyrosine ammonia lyase and hydroxycinnamic acid ligase activity in mesocotyls of maize inoculated with pathogenic fungi. Fitopatologia Brasileira 9(2): 376, 1984

l-Phenylalanine Ammonia-lyase (Maize): Partial Purification and Response to Gibberellic Acid and Cycloheximide of l-Phenylalanine and l-Tyrosine Ammonia-lyase Activities. Plant Physiology 50(4): 480-484, 1972

A phenylalanine ammonia-lyase from maize has also tyrosine ammonia-lyase activity. Experientia (Basel) 52(ABSTR ): A22, 1996

Effect of the brown midrib genes on the activity of peroxidase, phenylalanine ammonia-lyase, and tyrosine ammonia-lyase. Dissertation Abstracts International, B 36(10): 4790B, 1976

Identification by high-performance liquid chromatography of tyrosine ammonia-lyase activity in purified fractions of Phaseolus vulgaris phenylalanine ammonia-lyase. Journal of Chromatography 573(2): 309-312, 1992

Changes in the activity of phenylalanine ammonia-lyase (PAL), tyrosine ammonia-lyase and chalcone-flavanone isomerase in relation to the accumulation of C-glycosylflavones in developing shoots of oat seedlings (Avena sativa L.) in light and darkness. Zeitschrift fur Pflanzenphysiologie 74(3): 226-254, 1975

Leaf reddening in cotton genotypes. VI. Changes in phenylalanine ammonia lyase, tyrosine ammonia lyase activities and free phenols. Karnataka Journal of Agricultural Sciences 11(4): 908-915, 1998

Activities of phenylalanine ammonia-lyase (PAL) and tyrosine ammonia-lyase (TAL) in young rice panicles inoculated with Pyricularia grisea. Japanese Journal of Tropical Agriculture 42(1): 39-45, 1998

Chitosan and chitin oligomers increase phenylalanine ammonia-lyase and tyrosine ammonia-lyase activities in soybean leaves. Journal of Plant Physiology 160(8): 859-863, 2003