Summary
A large number of plant products of commercial value including essential amino acids, alkaloids, phenols and structural compounds are derived from the shikimate pathway, but it is poorly understood what control architectures are required to produce these compounds. The creation of transgenic plants with artificial metabolic sinks that produce shikimate derived end-products or which effectively down-regulate the production of others has been successfully used in our laboratory to eliminate tryptophan-derived indoleglucosinolates inBrassica napus(canola). The elimination of indoleglucosinolates in canola seeds would be useful since this could increase the palatability of canola protein meals which are used for feeding swine and poultry. We have also shown that important effects on aromatic amino acid levels are observed when artificial metabolic sinks for tryptophan are introduced into transgenic plants. Transgenic potatoes which express tryptophan decarboxylase accumulate significantly lower levels of tryptophan and these plants were used to evaluate if tryptophan might play a role in the regulation of the shikimate pathway. Tubers from trans-genic potatoes also accumulated significantly decreased levels of phenylalanine, accumulated reduced levels of soluble and wall-bound phenolic compounds after wounding and were significantly more susceptible to infection byPhytopthora infestansa major fungal pathogen of potato. The significance of these results will be discussed in relation to the evolution of control architectures in microorganisms, fungi and plants which may regulate the shikimate pathway and which may result in different adaptive responses observed in plants when they accommodate a new artificial metabolic sink.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
Altanassova, R.; Favet, N.; Martz, F.; Chabbert, B.; Tollier, M. T.; Monties, B.; Fritig, B.; Legrand, M. Altered lignin composition in transgenic tobacco expressing 0-methyltransferase sequences in sense and antisense orientation. The Plant Journal 1995, 8, 465–477.
Bailey, J.E. Toward a science of metabolic engineering. Science 1991, 253, 1668–1675.
Bate, N. J.; Orr, J.; Ni, W.; Meromi, A.; Nadler-Hassar, T.; Doemer, P. W.; Dixon, R. A.; Lamb, C. J.; Elkind, Y. Quantitative relationship between phenylalanine ammonia-lyase levels and phenylpropanoid accumulation in transgenic tobacco identifies a rate-determining step in natural product synthesis. Proc. Natl. Acad. Sci. USA 1994, 91, 7608–7612.
Bentley, R. The shikimate pathway-a metabolic tree with many branches. Crit. Rev. Biochem. Mol. Biol. 1990, 25, 307–384.
Berlin, J.; Rugenhagen, C.; Dietze, R; Fecker, L. F.; Goddijn, O. J. M.; Hoge, H. C. Increased production of serotonin by suspension cultures of Peganum harmala transformed with a tryptophan decarboxylase cDNA clone from Catharanthus roseus. Transgenic Research 1993, 2, 336–344.
Carsiotis, M.; Jones, R. F.; Wesseling, A. C. Cross-pathway regulation: histidine-mediated control of enzymes of histidine, tryptophan, and arginine biosynthetic enzymes in Neurospora crassa. Journal of Bacteriology 1974, 119, 893–898.
Chappell, C. C.; Vogt, T.; Ellis, B. E.; Somerville, C. R. An Arabidopsis mutant defective in the general phenylpropanoid pathway. Plant Cell 1992, 4, 1413–1424.
Chappell, C. C. A cDNA encoding a novel cytochrome P450-dependent monooxygenase from Arabidopsis thaliana. Plant Physiol. 1995, 108, 875–876.
Chavadej, S.; Brisson, N.; McNeil, J. N.; De Luca, V. Redirection of tryptophan leads to production of low indole glucosinolate canola. Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 2166–2170.
Demain A. L. Breaking through the gridlock on the aromatic thruway (to lower cost specialty chemicals), Nature Biotechnology 1996, 14, 582–583.
De Luca, V.; Marineau, C.; Brisson, N. Molecular cloning and analysis of cDNA encoding a plant tryptophan de-carboxylase: comparison with animal dopa decarboxylases. Proc. Natl. Acad. Sci. USA 1989, 86, 2582–2586.
De Luca, V. Molecular characterization of secondary metabolic pathways. AgBiotech. News and Information 1993, 5,225N–229N.
Dixon, R. A.; Paiva, N. Stress-induced phenylpropanoid metabolism. Plant Cell 1995, 7, 1085–1097.
Douglas, C. J. Phenylpropanoid metabolism and lignin biosynthesis: from weeds to trees. Trends in Plant Sciences 1996, 1, 171–178.
Eberhard, J.; Ehrler, T. T.; Epple, P.; Felix, G.; Raesecke, H. R.; Amrhein, N.; Schmid, J. Cytosolic and plastidic chorismate mutase isozymes from Arabidopsis thaliana: molecular characterization and enzymatic properties. Plant Journal 1996, 10, 815–821.
Flores, N.; Xiao, J.; Berry, A.; Bolivar, F.; Valle, F. Pathway engineering for the production of aromatic compounds in Escherichia coli. Nature Biotechnology 1996, 14, 620–623.
Goddijn, O. J. M.; Pen, J. Plants as Bioreactors. Trends in Biotechnology 1995, 13, 379–387.
Grand, C.; Parmentier, P.; Boudet, A.; Boudet, A. M. Comparison of lignins and of enzymes involved in lignification in normal and brown midrib mutant maize seedlings. Physiol. Veg. 1985, 23, 905–911.
Guyer, D.; Patton, D.; Ward, D. Evidence for cross-pathway regulation of metabolic gene expression in plants. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 4997–5000.
Halpin, C.; Knight, M. E.; Foxon, G. A.; Campbell, M. M.; Boudet, A. M.; Boon, J. J.; Chabbert, B.; Tollier, M. T.; Schuch, W. Manipulation of lignin quality by downregulation of cinnamyl alcohol dehydrogenase. The Plant Journal 1994, 6, 339–350.
Hibi, N.; Higashiguchi, S.; Hashimoto, T.; Yamada, Y. Gene expression in tobacco low-nicotine mutants. Plant Cell 1994, 6, 723–735.
Holton, T. A; Cornish, E. C. Genetics and biochemistry of anthocyanin biosynthesis. Plant Cell 1995, 7, 1071–1083.
Jensen, R. The shikimate/aerogenate pathway: link between carbohydrate metabolism and secondary metabolism. Physiol. Plantarum 1986, 66, 164–168.
Katsumata, R.; Ikeda, M. Hyperproduction of tryptophan in Corynebacterium glutamicum by pathway engineering. Bio/Technology 1993, 11, 921–925.
Kutchan, T. Alkaloid biosynthesis-the basis for metabolic engineering of medicinal plants. Plant Cell 1995, 7, 1069–1070.
Margna, U. Control at the level of substrate supply-an alternative in the regulation of phenylpropanoid accumulation in plant cells. Phytochemistry 1977, 16, 419–426.
McGarvey, D. J.; Croteau, R. Terpenoid metabolism. Plant Cell 1995, 7,1015–1026.
Nessler, C. L. Metabolic engineering of plant secondary products, Transgenic Research 1994, 3, 109–115.
Niederberger, P.; Miozzari, G.; Hutter, R. Biological role of the general control of amino acid biosynthesis in Saccharomyces cerevisiae. Molecular and Cellular Biology 1981, 1, 584–593.
Schmidt, J.; Amrhein, N. Molecular organization of the shikimate pathway in higher plants. Phytochemistry 1995, 39,737–749.
Vignols, F.; Rigau, J.; Torres, M. A.; Cappellades, M.; Puigdomènich, P. The brown midrib3 (bm3) mutant in maize occurs in the gene encoding caffeic acid O-methyltransferase. Plant Cell 1995, 7, 407–416.
Weiting, N.; Paiva, N.; Dixon, R. A. Reduced lignin in transgenic plants containing a caffeic acid 0-methyltransferase antisense gene. Transgenic Research 1994, 3, 120–126.
Whetten, R.; Sederoff, R. Lignin biosynthesis. Plant Cell 1995, 7, 1001–1013.
Yao, K.; De Luca, V.; Brisson, N. Creation of a metabolic sink for tryptophan alters the phenylpropanoid pathway and the susceptibility of potato to Phytopthora infestans. Plant Cell 1995, 7, 1787–1799.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1999 Springer Science+Business Media New York
About this chapter
Cite this chapter
De Luca, V. (1999). Production of Aromatic Amino Acid Derivatives through Metabolic Engineering of Crop Plants. In: Fu, TJ., Singh, G., Curtis, W.R. (eds) Plant Cell and Tissue Culture for the Production of Food Ingredients. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4753-2_3
Download citation
DOI: https://doi.org/10.1007/978-1-4615-4753-2_3
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-7155-7
Online ISBN: 978-1-4615-4753-2
eBook Packages: Springer Book Archive