| glutarate-semialdehyde dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.2.1.20 | ||||||||
| CAS no. | 9028-99-3 | ||||||||
| 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, a glutarate-semialdehyde dehydrogenase (EC 1.2.1.20) is an enzyme that catalyzes the chemical reaction
- glutarate semialdehyde + NAD+ + H2O glutarate + NADH + 2 H+
The 3 substrates of this enzyme are glutarate semialdehyde, NAD+, and H2O, whereas its 3 products are glutarate, 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 glutarate-semialdehyde:NAD+ oxidoreductase. This enzyme is also called glutarate semialdehyde dehydrogenase. This enzyme participates in lysine degradation.
References
- Ichihara A, Ichihara EA (February 1961). "Metabolism of L-lysine by bacterial enzymes. V. Glutaric semialdehyde dehydrogenase". Journal of Biochemistry. 49: 154–7. PMID 13717359.
This page was last edited on 26 August 2023, at 14:18