Download Amino Acids and their Derivatives in Higher Plants (Society by R. M. Wallsgrove (editor) PDF

By R. M. Wallsgrove (editor)

Vegetation convert inorganic nitrogen into amino acids, the development blocks for proteins. in addition they make quite a lot of different nitrogen compounds to aid defend themselves from pests and illnesses. An knowing of those compounds can hence assist in devising larger crop safeguard and construction tools. This quantity comprises essays by way of scientists who've studied facets of plant nitrogen nutrients and amino acid biosynthesis. There are chapters on protein amino acids, nonprotein amino acids, betaines, glutathione, polyamines, and different secondary metabolites derived from amino acids. the result of those reviews should be of curiosity to graduate scholars and execs in biochemistry and botany.

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Extra resources for Amino Acids and their Derivatives in Higher Plants (Society for Experimental Biology Seminar Series (No. 56))

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Chimeric genes included the 35S promoter and Q DNA sequence coding for the Q mRNA leader sequence with or without the transit peptide of the pea ribulose biphosphate carboxylase gene. Leaves of both types of transgenic plants exhibited a significant overproduction of free lysine or free threonine, respectively (Fig. 10). Accumulation of the essential amino acid was, in each case, positively correlated with the level of activity of the corresponding enzyme in a series of transgenic plants. Crop seeds generally contain very low levels of free threonine and lysine, amino acids which are often present in low amounts in seed protein.

E. (1982b). Threonine accumulation in the seeds of a barley mutant with an altered aspartate kinase. Biochemical Genetics, 20, 229^3. B. J. (1979b). Isolation of a recessive barley mutant resistant to S-(2-aminoethyl)-L-cysteine. Theoretical and Applied Genetics, 55, 1-4. , Degryse, E. & Jacobs, M. (1981). Selection and analysis of mutants overproducing amino acids of the aspartate family in barley, Arabidopsis and carrot. In Induced Mutations - A Tool in Plant Research (Proc. Symp. Vienna), pp.

L. W. (1989). Structure and expression of the maize gene encoding the phosphoenolpyruvate carboxylase isozyme involved in C4 photosynthesis. Plant Molecular Biology, 12, 579-89. , Yanagisawa, S. & Izui, K. (1992). Molecular evolution of phosphoenolpyruvate carboxylase for C4 photosynthesis in maize: comparison of its cDNA sequence with a newly isolated cDNA encoding an isozyme involved in the anaplerotic function. Journal of Biochemistry, 112, 147-54. Latzko, E. & Kelly, G. (1983). The many-faceted function of phosphoenolpyruvate carboxylase in C3 plant.

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