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- W142807682 abstract "Seeds of many crop plants are considered as a poor nutritional value food source, due to very low levels of the essential amino acid lysine. Attempts to increase lysine content in seeds are hampered by the presence of an active catabolic process that degrades lysine via saccharopine into other metabolites. The first enzyme in this catabolic process is lysine ketoglutarate reductase (LKR). We have recently obtained evidence that strongly suggest that lysine finely controls its own level in seeds by maintaining LKR activity balanced using two separate complementary mechanisms. I) LKR activity is post-translationally stimulated by lysine via a Ca+2 dependent intracellular signaling cascade that ends in the phosphorylation of the enzyme, thus, preventing lysine to accumulate to high levels. II) subsequent binding of lysine to the active site of the enzyme may expose phosphate residues on the surface of LKR rendering them more accessible to dephosphorylation, thus allowing lysine to accumulate to a sufficient level needed for protein synthesis." @default.
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- W142807682 date "1999-01-01" @default.
- W142807682 modified "2023-09-26" @default.
- W142807682 title "Regulation of Lysine Catabolism in Plants" @default.
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- W142807682 doi "https://doi.org/10.1007/978-94-011-4661-6_72" @default.
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