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 |
Enzyme Information
| 1.2.1.10 |
Acetaldehyde dehydrogenase (acetylating).
based on mapping to UniProt P9WQH3
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)
| P9WMK5 |
HOA_MYCTU
Mycobacterium tuberculosis H37Rv
4-hydroxy-2-oxovalerate aldolase
|
PDB Structure
| PDB | 4JN6 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Characterization of an Aldolase-Dehydrogenase Complex from the Cholesterol Degradation Pathway of Mycobacterium tuberculosis.
Biochemistry
|
