CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.360 | Dihydrodipicolinate Reductase; domain 2 |
|
3.30.360.10 | Dihydrodipicolinate Reductase; domain 2 |
Domain Context
CATH Clusters
| Superfamily | Dihydrodipicolinate Reductase; domain 2 |
| Functional Family | Bifunctional aspartokinase/homoserine dehydrogenase |
Enzyme Information
| 1.1.1.3 |
Homoserine dehydrogenase.
based on mapping to UniProt P31116
L-homoserine + NAD(P)(+) = L-aspartate 4-semialdehyde + NAD(P)H.
-!- The enzyme from Saccharomyces cerevisiae acts most rapidly with NAD(+); the Neurospora enzyme with NADP(+). -!- The enzyme from Escherichia coli is a multifunctional protein, which also catalyzes the reaction of EC 2.7.2.4.
|
UniProtKB Entries (1)
| P31116 |
DHOM_YEAST
Saccharomyces cerevisiae S288C
Homoserine dehydrogenase
|
PDB Structure
| PDB | 1EBF |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structures of homoserine dehydrogenase suggest a novel catalytic mechanism for oxidoreductases.
Nat.Struct.Biol.
|
