In enzymology, a saccharopine dehydrogenase (NADP+, L-glutamate-forming) () is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are saccharopine, oxidised nicotinamide adenine dinucleotide phosphate (NADP<sup>+</sup>), and water. Its products are L-glutamic acid, L-allysine, reduced NADPH, and a proton.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is N6-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-glutamate-forming). Other names in common use include 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), saccharopine reductase, 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase, and (L-glutamate-forming). This enzyme participates in lysine biosynthesis and lysine degradation.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes , , and .