Saccharopine dehydrogenase (NADP+, L-glutamate-forming)
| saccharopine dehydrogenase (NADP+, L-glutamate-forming) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.5.1.10 | ||||||||
| CAS number | 9033-55-0 | ||||||||
| 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 / EGO | ||||||||
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In enzymology, a saccharopine dehydrogenase (NADP+, L-glutamate-forming) (EC 1.5.1.10) is an enzyme that catalyzes the chemical reaction
- N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O L-glutamate + L-2-aminoadipate 6-semialdehyde + 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-glutamate, L-2-aminoadipate 6-semialdehyde, 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-glutamate-forming). Other names in common use include saccharopine (nicotinamide adenine dinucleotide phosphate,, glutamate-forming) dehydrogenase, aminoadipic semialdehyde-glutamic reductase, aminoadipate semialdehyde-glutamate reductase, aminoadipic semialdehyde-glutamate reductase, epsilon-N-(L-glutaryl-2)-L-lysine:NAD+(P) oxidoreductase, (L-2-aminoadipate-semialdehyde forming), saccharopine reductase, 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase, and (L-glutamate-forming). This enzyme participates in lysine biosynthesis and lysine degradation.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1E5L, 1E5Q, and 2AXQ.
References
- Jones EE, Broquist HP (1966). "Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. 3. Aminoadipic semialdehyde-glutamate reductase". J. Biol. Chem. 241 (14): 3430–4. PMID 4380448.