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 | Threonine dehydratase catabolic |
Enzyme Information
| 4.3.1.19 |
Threonine ammonia-lyase.
based on mapping to UniProt P11954
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 P11954
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)
| P11954 |
TDCB_SALTY
Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
L-threonine dehydratase catabolic TdcB
|
PDB Structure
| PDB | 2GN2 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structures of Salmonella typhimurium biodegradative threonine deaminase and its complex with CMP provide structural insights into ligand-induced oligomerization and enzyme activation.
J.Biol.Chem.
|