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saccharopine/zea mays
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Purification and Characterization of the Bifunctional Enzyme Lysine-Ketoglutarate Reductase-Saccharopine Dehydrogenase from Maize.
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The first enzyme of the lysine degradation pathway in maize (Zea mays L.), lysine-ketoglutarate reductase, condenses lysine and [alpha]-ketoglutarate into saccharopine using NADPH as a cofactor, whereas the second, saccharopine dehydrogenase, converts saccharopine to
Partial purification and characterization of lysine-ketoglutarate reductase in normal and opaque-2 maize endosperms.
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Lysine-ketoglutarate reductase catalyzes the first step of lysine catabolism in maize (Zea mays L.) endosperm. The enzyme condenses l-lysine and alpha-ketoglutarate into saccharopine using NADPH as cofactor. It is endosperm-specific and has a temporal pattern of activity, increasing with the onset
The bifunctional LKR/SDH locus of plants also encodes a highly active monofunctional lysine-ketoglutarate reductase using a polyadenylation signal located within an intron.
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Both plants and animals catabolize lysine (Lys) via two consecutive enzymes, Lys-ketoglutarate reductase (LKR) and saccharopine dehydrogenase (SDH), which are linked on a single polypeptide encoded by a single LKR/SDH gene. We have previously shown that the Arabidopsis LKR/SDH gene also encodes a
Lysine-ketoglutarate reductase activity in developing maize endosperm.
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Lysine-ketoglutarate reductase activity was detected and characterized in the developing endosperm of maize (Zea mays L.). The enzyme showed specificity for its substrates: lysine, alpha-ketoglutarate, and NADPH. Formation of the reaction product saccharopine was demonstrated. The pH optimum of the
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