CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.720 | NAD(P)-binding Rossmann-like Domain |
Domain Context
CATH Clusters
| Superfamily | NAD(P)-binding Rossmann-like Domain |
| Functional Family | L-threonine 3-dehydrogenase, mitochondrial |
Enzyme Information
| 1.1.1.103 |
L-threonine 3-dehydrogenase.
based on mapping to UniProt Q8K3F7
L-threonine + NAD(+) = L-2-amino-3-oxobutanoate + NADH.
-!- Acts in concert with EC 2.3.1.29 in the degradation of threonine to glycine. -!- This threonine-degradation pathway is common to prokaryotic and eukaryotic cells and the two enzymes involved form a complex. -!- In aqueous solution, the product L-2-amino-3-oxobutanoate can spontaneously decarboxylate to form aminoacetone.
|
UniProtKB Entries (1)
| Q8K3F7 |
TDH_MOUSE
Mus musculus
L-threonine 3-dehydrogenase, mitochondrial
|
PDB Structure
| PDB | 4YRB |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural insights on mouse l-threonine dehydrogenase: A regulatory role of Arg180 in catalysis
J.Struct.Biol.
|