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
| 4.3.1.19 |
Threonine ammonia-lyase.
based on mapping to UniProt Q96GA7
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.
|
| 4.3.1.17 |
L-serine ammonia-lyase.
based on mapping to UniProt Q96GA7
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.
|
UniProtKB Entries (1)
| Q96GA7 |
SDSL_HUMAN
Homo sapiens
Serine dehydratase-like
|
PDB Structure
| PDB | 2RKB |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
A catalytic mechanism that explains a low catalytic activity of serine dehydratase like-1 from human cancer cells: Crystal structure and site-directed mutagenesis studies.
Biochim.Biophys.Acta
|