| 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 | ||||||||
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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
glutarate + NADH + 2 HThe 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.
| Aldehyde/oxo oxidoreductases (EC 1.2) | |
|---|---|
| 1.2.1: NAD or NADP | |
| 1.2.2: cytochrome | |
| 1.2.3: oxygen | |
| 1.2.4: disulfide | |
| 1.2.7: iron–sulfur protein | |
| Enzymes | |
|---|---|
| Activity | |
| Regulation | |
| Classification | |
| Kinetics | |
| Types |
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