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References
Markovitz, P.J.; Chuang, D.T.: The bifunctional aminoadipic semialdehyde synthase in lysine degradation. Separation of reductase and dehydrogenase domains by limited proteolysis and column chromatography. J. Biol. Chem., 262, 9353–9358 (1987)
Fjellstedt, T.A.; Robinson, J.C.: Properties of partially purified saccharopine dehydrogenase from human placenta. Arch. Biochem. Biophys., 171, 191–196 (1975)
Hutzler, J.; Dancis, J.: Lysine-ketoglutarate reductase in human tissues. Biochim. Biophys. Acta, 377, 42–51 (1975)
Fellows, F.C.I.; Lewis, M.H.R.: Lysine metabolism in mammals. Biochem. J., 136, 329–334 (1973)
Hutzler, J.; Dancis, J.: Saccharopine cleavage by a dehydrogenase of human liver. Biochim. Biophys. Acta, 206, 205–214 (1970)
Mukhopadhyay, A.; Mungre, S.M.; Desmukh, D.R.: Comparison of lysine and tryptophan catabolizing enzymes in rat and bovine tissues. Experientia, 46, 874–876 (1990)
Markovitz, P.J.; Chuang, D.T.; Cox, R.P.: Familial hyperlysinemias. Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities. J. Biol. Chem., 259, 11643–11646 (1984)
Blemings, K.P.; Crenshaw, T.D.; Swick, R.W.; Benevenga, N.J.: Lysine-α-ketoglutarate reductase and saccharopine dehydrogenase are located only in the mitochondrial matrix in rat liver. J. Nutr., 124, 1215–1221 (1994)
Goncalves-Butruille, M.; Szajner, P.; Torigoi, E.; Leite, A.; Arruda, P.: Purification and characterization of the bifunctional enzyme lysine-ketoglutarate reductase-saccharopine dehydrogenase from maize. Plant Physiol., 110, 765–771. (1996)
Gaziola, S.A.; Teixeira, C.M.; Lugli, J.; Sodek, L.; Azevedo, R.A.: The enzymology of lysine catabolism in rice seeds. Isolation, characterization, and regulatory properties of a lysine 2-oxoglutarate reductase/saccharopine dehydrogenase bifunctional polypeptide. Eur. J. Biochem., 247, 364–371. (1997)
Miron, D.; Ben-Yaacov, S.; Karchi, H.; Galili, G.: In vitro dephosphorylation inhibits the activity of soybean lysine-ketoglutarate reductase in a lysineregulated manner. Plant J., 12, 1453–1458 (1997)
Zhu, X.; Tang, G.; Galili, G.: Characterization of the two saccharopine dehydrogenase isozymes of lysine catabolism encoded by the single composite AtLKR/SDH locus of Arabidopsis. Plant Physiol., 124, 1363–1371 (2000)
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(2005). Saccharopine dehydrogenase (NAD+, l-glutamate-forming). In: Schomburg, D., Schomburg, I. (eds) Springer Handbook of Enzymes. Springer Handbook of Enzymes, vol 23. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-37648-8_9
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DOI: https://doi.org/10.1007/3-540-37648-8_9
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