CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.1100 |
Domain Context
CATH Clusters
| Superfamily | 3.40.50.1100 |
| Functional Family | D-serine dehydratase |
Enzyme Information
| 4.3.1.18 |
D-serine ammonia-lyase.
based on mapping to UniProt P00926
D-serine = pyruvate + NH(3).
-!- The enzyme cleaves a carbon-oxygen bond, releasing a water molecule (hence the enzyme's original classification as EC 4.2.1.14) and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. -!- The latter reaction, which can occur spontaneously, can also be catalyzed by EC 3.5.99.10. -!- Also acts, slowly, on D-threonine. -!- Formerly EC 4.2.1.14.
|
UniProtKB Entries (1)
| P00926 |
SDHD_ECOLI
Escherichia coli K-12
D-serine dehydratase
|
PDB Structure
| PDB | 3SS9 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of D-serine dehydratase from Escherichia coli.
Biochim.Biophys.Acta
|
