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

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In enzymology, a saccharopine dehydrogenase (NAD+, L-lysine-forming) (EC 1.5.1.7) is an enzyme that catalyzes the chemical reaction

N₆-(L-1,3-dicarboxypropyl)-L-lysine + NAD⁺ + H₂O $\rightleftharpoons$ L-lysine + 2-oxoglutarate + 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-lysine, 2-oxoglutarate, 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-lysine-forming). Other names in common use include lysine-2-oxoglutarate reductase, dehydrogenase, saccharopine (nicotinamide adenine dinucleotide,, lysine forming), epsilon-N-(L-glutaryl-2)-L-lysine:NAD oxidoreductase (L-lysine, forming), N6-(glutar-2-yl)-L-lysine:NAD oxidoreductase (L-lysine-forming), 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase, and (L-lysine-forming). This enzyme participates in lysine biosynthesis and lysine degradation.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1FF9.

[edit] References

IUBMB entry for 1.5.1.7
BRENDA references for 1.5.1.7 (Recommended.)
PubMed references for 1.5.1.7
PubMed Central references for 1.5.1.7
Google Scholar references for 1.5.1.7
Fujioka M, Nakatani Y (1972). "Saccharopine dehydrogenase. Interaction with substrate analogues". Eur. J. Biochem. 25: 301–7. doi:10.1111/j.1432-1033.1972.tb01697.x. PMID 4339117.
Saunders PP, Broquist HP (1966). "Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. IV. Saccharopine dehydrogenase". J. Biol. Chem. 241: 3435–40. PMID 4287986.