CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.360 | Dihydrodipicolinate Reductase; domain 2 |
|
3.30.360.10 | Dihydrodipicolinate Reductase; domain 2 |
Domain Context
CATH Clusters
| Superfamily | Dihydrodipicolinate Reductase; domain 2 |
| Functional Family | Acetaldehyde dehydrogenase |
Enzyme Information
| 1.2.1.10 |
Acetaldehyde dehydrogenase (acetylating).
based on mapping to UniProt Q52060
Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH.
-!- Also acts, more slowly, on glycolaldehyde, propanal and butanal. -!- In several bacterial species this enzyme forms a bifunctional complex with EC 4.1.3.39. -!- The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 1.2.1.87. -!- Involved in the meta-cleavage pathway for the degradation of phenols, methylphenols and catechols. -!- NADP(+) can replace NAD(+) but the rate of reaction is much slower.
|
UniProtKB Entries (1)
| P51016 |
HOA_PSEUF
Pseudomonas sp. CF600
4-hydroxy-2-oxovalerate aldolase
|
PDB Structure
| PDB | 1NVM |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of a bifunctional aldolase-dehydrogenase: Sequestering a
reactive and volatile intermediate
Proc.Natl.Acad.Sci.USA
|
