L-aminoadipate-semialdehyde dehydrogenase
In enzymology, a L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31) is an enzyme that catalyzes the chemical reaction
- L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O L-2-aminoadipate + NAD(P)H + H+
| L-aminoadipate-semialdehyde dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Alpha-aminoadipic semialdehyde dehydrogenase tetramer, Human | |||||||||
| Identifiers | |||||||||
| EC number | 1.2.1.31 | ||||||||
| CAS number | 9067-87-2 | ||||||||
| 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 | ||||||||
| |||||||||
The 4 substrates of this enzyme are L-2-aminoadipate 6-semialdehyde, NAD+, NADP+, and H2O, whereas its 4 products are L-2-aminoadipate, NADH, NADPH, and H+.
This enzyme participates in lysine biosynthesis and biodegradation.
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-2-aminoadipate-6-semialdehyde:NAD(P)+ 6-oxidoreductase. Other names in common use include:
- aminoadipate semialdehyde dehydrogenase,
- 2-aminoadipate semialdehyde dehydrogenase,
- alpha-aminoadipate-semialdehyde dehydrogenase,
- alpha-aminoadipate reductase,
- 2-aminoadipic semialdehyde dehydrogenase,
- L-alpha-aminoadipate delta-semialdehyde oxidoreductase,
- L-alpha-aminoadipate delta-semialdehyde:NAD+ oxidoreductase,
- L-alpha-aminoadipate delta-semialdehyde:nicotinamide adenine,
- and dinucleotide oxidoreductase.
References
- Calvert AF, Rodwell VW (1966). "Metabolism of pipecolic acid in a Pseudomonas species. 3 L-alpha-aminoadipate delta-semialdehyde:nicotinamide adenine dinucleotide oxidoreductase". J. Biol. Chem. 241 (2): 409–14. PMID 4285660.
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