Saccharopine dehydrogenase (NAD+, L-glutamate-forming)
| saccharopine dehydrogenase (NAD+, L-glutamate-forming) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.5.1.9 | ||||||||
| CAS no. | 37256-26-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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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 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.
References
- Hutzler J, Dancis J (1968). "Conversion of lysine to saccharopine by human tissues". Biochim. Biophys. Acta. 158 (1): 62–9. doi:10.1016/0304-4165(68)90072-x. 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 (19): 11643–6. PMID 6434529.
