saccharopine dehydrogenase (NADP+, L-glutamate-forming)
saccharopine (nicotinamide adenine dinucleotide phosphate,glutamate-forming) dehydrogenase
aminoadipic semialdehyde-glutamic reductase
aminoadipate semialdehyde-glutamate reductase
aminoadipic semialdehyde-glutamate reductase
epsilon-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase(L-2-aminoadipate-semialdehyde forming)
6-N-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase(L-glutamate-forming)
Properties of partially purified saccharopine dehydrogenase from human placenta.
Phylogenetic analyses of proton-translocating transhydrogenases.
Crystal structure of saccharopine reductase from Magnaporthe grisea, an enzyme of the alpha-aminoadipate pathway of lysine biosynthesis.
The activity of the Arabidopsis bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase enzyme of lysine catabolism is regulated by functional interaction between its two enzyme domains.
Saccharopine Dehydrogenases are a collective term for the enzymes that use either NAD+ (EC 1.5.1.7) or NADP+ (EC 1.5.1.8) as an acceptor to form L-lysine, or NAD+ (EC 1.5.1.9) or NADP+ (EC 1.5.1.10) as an acceptor to form L-glutamate. According to the paper [3], this enzyme catalyzes three different reactions, addition to double-bond, elimination accompanied by double-bond formation, and reduction.