Nitrogen Metabolism in Plants in the Post-genomic Era by Christine Foyer, Hanma Zhang

By Christine Foyer, Hanma Zhang

Nitrogen Metabolism in vegetation presents a basic heritage and assessment of nitrogen acquisition in vegetation and provides a entire description of modern advances in our figuring out of either nitrogen assimilation and nitrogen fixation utilizing new applied sciences. this crucial new e-book covers many very important points, together with delivery platforms, regulatory and signaling mechanisms, plant improvement and senescence, and metabolic cross-talk among nitrogen assimilation and different metabolic pathways. a part of Wiley-Blackwell's hugely acclaimed and profitable Annual Plant reports, this new quantity is a necessary buy for all plant scientists.

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2004). Good et al. (2007) transformed canola (Brassica napus) with an alanine dehydrogenase cDNA under the control of a root-specific promoter. The transgenic plants had increased biomass and seed yield, both in the laboratory and the field, under low N conditions, whereas no differences were observed under high N. The results suggested that the transgenics required 40% less applied nitrogen fertilizer to achieve yields similar to the wild type. 4 Conclusions The research reviewed here has tended to confirm the generalities of the established biochemical pathways for N assimilation and cycling around the plant.

C01 BLBK316-Foyer 10 August 25, 2010 16:28 Trim: 234mm×156mm Series: APR Char Count= Nitrogen Metabolism in Plants in the Post-genomic Era of GS activity is at the transcriptional level (see above and Miflin & Habash, 2002). These regulatory processes are presumably under the influence of further sets of genes which generate yet another layer of genetic complexity of N metabolism. 2 Glutamate synthase The second enzyme involved in ammonia assimilation is glutamate synthase, also known as glutamine:2-oxoglutarate amidotransferase (GOGAT).

Borek et al. , 1999) in E. coli. The recombinant native enzyme had a molecular mass of 75 kDa, but the peptide underwent an autoproteolytic cleavage, leading to the formation of two subunits of 23 kDa (␣-subunit) and 14 kDa (␤-subunit), confirming the existence of the (␣␤)2 -tetramer. This cleavage gives rise to an N-terminal nucleophilic threonine residue on the ␤-subunit. Phylogenetic analysis of N-terminal nucleophilic hydrolases indicated that the amino acid sequences of the plant asparaginases from A.

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