Saccharopine dehydrogenase (NADP+, L-lysine-forming)

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In enzymology, a saccharopine dehydrogenase (NADP+, L-lysine-forming) (EC 1.5.1.8) is an enzyme that catalyzes the chemical reaction

N₆-(L-1,3-dicarboxypropyl)-L-lysine + NADP⁺ + H₂O $\rightleftharpoons$ L-lysine + 2-oxoglutarate + NADPH + H⁺

The 3 substrates of this enzyme are N6-(L-1,3-dicarboxypropyl)-L-lysine, NADP⁺, and H₂O, whereas its 4 products are L-lysine, 2-oxoglutarate, NADPH, 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:NADP+ oxidoreductase (L-lysine-forming). Other names in common use include lysine-2-oxoglutarate reductase, lysine-ketoglutarate reductase, L-lysine-alpha-ketoglutarate reductase, lysine:alpha-ketoglutarate:TPNH oxidoreductase, (epsilon-N-[gultaryl-2]-L-lysine forming), saccharopine (nicotinamide adenine dinucleotide phosphate,, lysine-forming) dehydrogenase, 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase, and (L-lysine-forming). This enzyme participates in lysine biosynthesis and lysine degradation.

[edit] References

IUBMB entry for 1.5.1.8
BRENDA references for 1.5.1.8 (Recommended.)
PubMed references for 1.5.1.8
PubMed Central references for 1.5.1.8
Google Scholar references for 1.5.1.8
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.