In enzymology, a succinate-semialdehyde dehydrogenase (SSADH) (EC 1.2.1.24) is an enzyme that catalyzes the chemical reaction
| 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 PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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- succinate semialdehyde NAD H2O ⇌ succinate NADH 2 H
The 3 substrates of this enzyme are succinate semialdehyde, NAD , and H2O, whereas its 3 products are succinate, NADH, and H .
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 succinate-semialdehyde:NAD oxidoreductase. Other names in common use include succinate semialdehyde dehydrogenase, succinic semialdehyde dehydrogenase, succinyl semialdehyde dehydrogenase, and succinate semialdehyde:NAD oxidoreductase. This enzyme participates in glutamate and butyrate metabolism.
Succinate-semialdehyde dehydrogenase is found in organisms ranging across the tree of life from bacteria to humans. It is important in the degradation of γ-aminobutyric acid in humans, and deficiency of the enzyme causes serious health effects (succinic semialdehyde dehydrogenase deficiency).
In bacteria, the enzyme is also involved in γ-aminobutyric acid degradation, but can be recruited to facilitate other functions, such as converting succinate-semialdehyde formed during fission of the pyridine ring to succinic acid for entry into the Krebs Cycle.[1]
References
edit- ^ Sims GK, Sommers LE, Konopka A (May 1986). "Degradation of Pyridine by Micrococcus luteus Isolated from Soil". Appl. Environ. Microbiol. 51 (5): 963–968. PMC 238995. PMID 16347070.963-968&rft.date=1986-05&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC238995#id-name=PMC&rft_id=info:pmid/16347070&rft.aulast=Sims&rft.aufirst=GK&rft.au=Sommers, LE&rft.au=Konopka, A&rft_id=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC238995&rfr_id=info:sid/en.wikipedia.org:Succinate-semialdehyde dehydrogenase" class="Z3988">
Further reading
edit- ALBERS RW, KOVAL GJ (1961). "Succinic semialdehyde dehydrogenase: purification and properties of the enzyme from monkey brain". Biochim. Biophys. Acta. 52: 29–35. doi:10.1016/0006-3002(61)90900-3. PMID 13860092.29-35&rft.date=1961&rft_id=info:doi/10.1016/0006-3002(61)90900-3&rft_id=info:pmid/13860092&rft.aulast=ALBERS&rft.aufirst=RW&rft.au=KOVAL, GJ&rfr_id=info:sid/en.wikipedia.org:Succinate-semialdehyde dehydrogenase" class="Z3988">
