Succinate-semialdehyde dehydrogenase (NAD(P)+)
| succinate-semialdehyde dehydrogenase [NAD(P)+] | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.1.16 | ||||||||
| CAS no. | 37250-88-7 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, succinate-semialdehyde dehydrogenase [NAD(P)+] (EC 1.2.1.16) is an enzyme that catalyzes the chemical reaction
The three substrates of this enzyme are succinic semialdehyde, oxidised nicotinamide adenine dinucleotide (NAD+) and water. Its products are succinic acid, reduced NADH, and a proton. This enzyme can use the alternative cofactor, nicotinamide adenine dinucleotide phosphate.[1][2][3]
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(P)+ oxidoreductase. Other names in common use include succinate semialdehyde dehydrogenase (nicotinamide adenine, dinucleotide (phosphate)), and succinate-semialdehyde dehydrogenase [NAD(P)+]. This enzyme participates in 3 metabolic pathways: glutamate metabolism, tyrosine metabolism, and butanoate metabolism.[4]
See also
- Succinate-semialdehyde dehydrogenase which catalyses the same reaction
References
- ^ Enzyme 1.2.1.16 at KEGG Pathway Database.
- ^ JAKOBY WB, SCOTT EM (1959). "Aldehyde oxidation. III. Succinic semialdehyde dehydrogenase". J. Biol. Chem. 234 (4): 937–40. doi:10.1016/S0021-9258(18)70207-X. PMID 13654295.
- ^ Nirenberg MW; Jakoby WB (1960). "Enzymatic utilization of gamma-hydroxybutyric acid". J. Biol. Chem. 235 (4): 954–960. doi:10.1016/S0021-9258(18)69459-1. PMID 14427301.
- ^ Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 203-221.