CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.20 | TIM Barrel |
|
3.20.20.60 | Phosphoenolpyruvate-binding domains |
Domain Context
CATH Clusters
| Superfamily | Phosphoenolpyruvate-binding domains |
| Functional Family | 5-keto-4-deoxy-D-glucarate aldolase |
Enzyme Information
| 4.1.2.52 |
4-hydroxy-2-oxoheptanedioate aldolase.
based on mapping to UniProt Q47098
4-hydroxy-2-oxoheptanedioate = pyruvate + succinate semialdehyde.
-!- The enzyme is also able to catalyze the aldol cleavage of 4-hydroxy- 2-oxopentanoate and 4-hydroxy-2-oxohexanoate, and can use 2-oxobutanoate as carbonyl donor, with lower efficiency. -!- In the reverse direction, is able to condense a range of aldehyde acceptors with pyruvate. -!- The enzyme from the bacterium Escherichia coli produces a racemic mixture of (4R)- and (4S)-hydroxy-2-oxoheptanedioate. -!- Formerly EC 4.1.2.n4.
|
UniProtKB Entries (1)
| Q47098 |
HPCH_ECOLX
Escherichia coli
4-hydroxy-2-oxo-heptane-1,7-dioate aldolase
|
PDB Structure
| PDB | 2V5J |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure and Mechanism of Hpch: A Metal Ion Dependent Class II Aldolase from the Homoprotocatechuate Degradation Pathway of Escherichia Coli.
J.Mol.Biol.
|
