| Acetaldehyde dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Pseudomonas sp. aldolase-dehydrogenase heterotetramer assembly consisting of 4-hydroxy-2-ketovalerate aldolase (blue) and acetaldehyde dehydrogenase (red). PDB: 1NVM[1] | |||||||||
| Identifiers | |||||||||
| EC no. | 1.2.1.10 | ||||||||
| CAS no. | 9028-91-5 | ||||||||
| 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 | ||||||||
| |||||||||
Acetaldehyde dehydrogenases (EC 1.2.1.10) are dehydrogenase enzymes which catalyze the conversion of acetaldehyde into acetyl-CoA. This can be summarized as follows:
Acetaldehyde + NAD+ + Coenzyme A ↔ Acetyl-CoA + NADH + H+
In humans, there are three known genes which encode this enzymatic activity, ALDH1A1, ALDH2, and the more recently discovered ALDH1B1 (also known as ALDH5). These enzymes are members of the larger class of aldehyde dehydrogenases.
The CAS number for this type of the enzyme is [9028-91-5].
- ^ PDB: 1NVM; Manjasetty BA, Powlowski J, Vrielink A (Jun 2003). "Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate". Proceedings of the National Academy of Sciences of the United States of America. 100 (12): 6992–7. Bibcode:2003PNAS..100.6992M. doi:10.1073/pnas.1236794100. PMC 165818. PMID 12764229.