Saccharopine_dehydrogenase_(NAD+,_L-lysine-forming)

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

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

Add article description


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 L-lysine + 2-oxoglutarate + NADH + H+
Quick Facts Identifiers, EC no. ...

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.

Structural studies

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


References

    • Fujioka M, Nakatani Y (1972). "Saccharopine dehydrogenase. Interaction with substrate analogues". Eur. J. Biochem. 25 (2): 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 (14): 3435–40. PMID 4287986.



    Share this article:

    This article uses material from the Wikipedia article Saccharopine_dehydrogenase_(NAD+,_L-lysine-forming), and is written by contributors. Text is available under a CC BY-SA 4.0 International License; additional terms may apply. Images, videos and audio are available under their respective licenses.