Biology:Saccharopine dehydrogenase (NADP+, L-lysine-forming)
| saccharopine dehydrogenase (NADP+, L-lysine-forming) | |||||||||
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| Identifiers | |||||||||
| EC number | 1.5.1.8 | ||||||||
| CAS number | 9031-19-0 | ||||||||
| 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 (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 [math]\displaystyle{ \rightleftharpoons }[/math] 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.
References
- "Conversion of lysine to saccharopine by human tissues". Biochim. Biophys. Acta 158 (1): 62–9. 1968. doi:10.1016/0304-4165(68)90072-x. PMID 4385118.
- "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. 1984. PMID 6434529.
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