Saccharopine dehydrogenase (NAD+, L-glutamate-forming)

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In enzymology, a saccharopine dehydrogenase (NAD+, L-glutamate-forming) (EC 1.5.1.9) is an enzyme that catalyzes the chemical reaction

N₆-(L-1,3-dicarboxypropyl)-L-lysine + NAD⁺ + H₂O $\rightleftharpoons$ L-glutamate + 2-aminoadipate 6-semialdehyde + NADH + H⁺

The 3 substrates of this enzyme are N6-(L-1,3-dicarboxypropyl)-L-lysine, NAD⁺, and H₂O, whereas its 4 products are L-glutamate, 2-aminoadipate 6-semialdehyde, NADH, and H⁺.

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:NAD+ oxidoreductase (L-glutamate-forming). Other names in common use include dehydrogenase, saccharopine (nicotinamide adenine dinucleotide,, glutamate-forming), saccharopin dehydrogenase, NAD+ oxidoreductase (L-2-aminoadipic-delta-semialdehyde and, glutamate forming), aminoadipic semialdehyde synthase, saccharopine dehydrogenase (NAD+, L-glutamate-forming), 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase, and (L-glutamate-forming). This enzyme participates in lysine degradation.

[edit] References

IUBMB entry for 1.5.1.9
BRENDA references for 1.5.1.9 (Recommended.)
PubMed references for 1.5.1.9
PubMed Central references for 1.5.1.9
Google Scholar references for 1.5.1.9
Hutzler J, Dancis J (1968). "Conversion of lysine to saccharopine by human tissues". Biochim. Biophys. Acta. 158: 62–9. PMID 4385118.
Markovitz PJ, Chuang DT, Cox RP (1984). "Familial hyperlysinemias. Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities". J. Biol. Chem. 259: 11643–6. PMID 6434529.