CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.640 | Aspartate Aminotransferase; domain 2 |
|
3.40.640.10 | Type I PLP-dependent aspartate aminotransferase-like (Major domain) |
Domain Context
CATH Clusters
| Superfamily | Type I PLP-dependent aspartate aminotransferase-like (Major domain) |
| Functional Family | Low-specificity L-threonine aldolase |
Enzyme Information
| 4.1.2.48 |
Low-specificity L-threonine aldolase.
based on mapping to UniProt P75823
(1) L-threonine = glycine + acetaldehyde. (2) L-allo-threonine = glycine + acetaldehyde.
-!- The low-specificity L-threonine aldolase can act on both L-threonine and L-allo-threonine. -!- The enzyme from Escherichia coli can also act on L-threo-phenylserine and L-erythro-phenylserine. -!- The enzyme can also catalyze the aldol condensation of glycolaldehyde and glycine to form 4-hydroxy-L-threonine, an intermediate of pyridoxal phosphate biosynthesis. -!- Different from EC 4.1.2.5 and EC 4.1.2.49.
|
UniProtKB Entries (1)
| P75823 |
LTAE_ECOLI
Escherichia coli K-12
Low specificity L-threonine aldolase
|
PDB Structure
| PDB | 3WLX |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure analysis of L-threonine aldolase from Escherichia coli unravels the low-specificity and thermostability
To be Published
|
