CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.1020 | Biosynthetic Threonine Deaminase; domain 3 |
|
3.40.1020.10 | Biosynthetic Threonine Deaminase; Domain 3 |
Domain Context
CATH Clusters
| Superfamily | Biosynthetic Threonine Deaminase; Domain 3 |
| Functional Family | L-threonine dehydratase |
Enzyme Information
| 4.3.1.19 |
Threonine ammonia-lyase.
based on mapping to UniProt P04968
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)
| P04968 |
ILVA_ECOLI
Escherichia coli K-12
L-threonine dehydratase biosynthetic IlvA
|
PDB Structure
| PDB | 1TDJ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase.
Structure
|