| succinate-semialdehyde dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Succinate semialdehyde dehydrogenase dodecamer, Human | |||||||||
| Identifiers | |||||||||
| EC no. | 1.2.1.24 | ||||||||
| CAS no. | 9028-95-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDBPDBePDBsum | ||||||||
| Gene Ontology | AmiGO /QuickGO | ||||||||
| |||||||||
Inenzymology,succinate-semialdehyde dehydrogenase (SSADH) (EC1.2.1.24) is anenzyme thatcatalyzes thechemical reaction
The threesubstrates of this enzyme are succinic semialdehyde, oxidisednicotinamide adenine dinucleotide (NAD+), and water. Itsproducts are succinic acid, reduced NADH, and aproton.[1][2]
This enzyme belongs to the family ofoxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. Thesystematic name of this enzyme class issuccinate-semialdehyde:NAD+ oxidoreductase. Other names in common use includesuccinate semialdehyde dehydrogenase,succinic semialdehyde dehydrogenase,succinyl semialdehyde dehydrogenase, andsuccinate semialdehyde:NAD+ oxidoreductase. This enzyme participates inglutamate andbutyrate metabolism.
Succinate-semialdehyde dehydrogenase is found in organisms ranging across the tree of life from bacteria to humans. It is important in the degradation ofγ-aminobutyric acid in humans, and deficiency of the enzyme causes serious health effects (succinic semialdehyde dehydrogenase deficiency).
In bacteria, the enzyme is also involved inγ-aminobutyric acid degradation, but can be recruited to facilitate other functions, such as converting succinate-semialdehyde formed during fission of thepyridine ring to succinic acid for entry into theKrebs Cycle.[3]
