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 | L-serine dehydratase/L-threonine deaminase |
Enzyme Information
| 4.3.1.17 |
L-serine ammonia-lyase.
based on mapping to UniProt P20132
L-serine = pyruvate + NH(3).
-!- The reaction catalyzed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.13) followed by tautomerization to an imine form and hydrolysis of the C-N bond. -!- The latter reaction, which can occur spontaneously, is also be catalyzed by EC 3.5.99.10. -!- This reaction is also carried out by EC 4.3.1.19 from a number of sources. -!- Formerly EC 4.2.1.13.
|
| 4.3.1.19 |
Threonine ammonia-lyase.
based on mapping to UniProt P20132
L-threonine = 2-oxobutanoate + NH(3).
-!- The reaction catalyzed by both types of enzymes involves the initial elimination of water to form an enamine intermediate (hence the enzyme's original classification as EC 4.2.1.16), followed by tautomerization to an imine form and hydrolysis of the C-N bond. -!- The latter reaction, which can occur spontaneously, is also be catalyzed by EC 3.5.99.10. -!- The enzymes from a number of sources also act on L-serine, cf. EC 4.3.1.17. -!- Formerly EC 4.2.1.16.
|
UniProtKB Entries (1)
| P20132 |
SDHL_HUMAN
Homo sapiens
L-serine dehydratase/L-threonine deaminase
|
PDB Structure
| PDB | 1P5J |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystallization and preliminary crystallographic analysis of human serine dehydratase.
Acta Crystallogr.,Sect.D
|
