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Maize Phenylalanine Ammonia-Lyase Has Tyrosine Ammonia-Lyase Activity
Open accessAbstract
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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Cited by
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Role of bifunctional ammonia-lyase in grass cell wall biosynthesis
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Schenck, C. A., & Maeda, H. A. (2018) · Phytochemistry · doi:10.1016/j.phytochem.2018.02.003 · Cited by 286
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Metadata
- Authors
- Rosler, J., Krekel, F., Amrhein, N., & Schmid, J.
- Venue
- Plant Physiology
- Publisher
- Oxford University Press (OUP)
- Published
- 1997-01-01
- Volume
- 113
- Issue
- 1
- Pages
- 175-179
- ISSN
- 0032-0889 (ISSN-L)
- 1532-2548
- OpenAlex
- W2026031369
- Cited by
- 359
- References
- 0
- FWCI
- 1.24
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Rosler, J., Krekel, F., Amrhein, N., & Schmid, J. (1997). Maize Phenylalanine Ammonia-Lyase Has Tyrosine Ammonia-Lyase Activity. Plant Physiology. https://doi.org/10.1104/pp.113.1.175
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