CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.910 | Deoxyhypusine Synthase |
|
3.40.910.10 | Deoxyhypusine synthase |
Domain Context
CATH Clusters
| Superfamily | Deoxyhypusine synthase |
| Functional Family | deoxyhypusine synthase isoform X2 |
Enzyme Information
| 2.5.1.46 |
Deoxyhypusine synthase.
based on mapping to UniProt P49366
[eIF5A-precursor]-lysine + spermidine = [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine.
-!- The eukaryotic initiation factor eIF5A contains a hypusine residue that is essential for activity. -!- Catalyzes the first reaction of hypusine formation from one specific lysine residue of the eIF5A precursor. -!- The reaction occurs in four steps: NAD(+)-dependent dehydrogenation of spermidine (1a), formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue (1b), transfer of the same 4-aminobutylidene group from the enzyme intermediate to the e1F5A precursor (1c), reduction of the e1F5A-imine intermediate to form a deoxyhypusine residue (1d). -!- Hence the overall reaction is transfer of a 4-aminobutyl group. -!- For the plant enzyme, homospermidine can substitute for spermidine and putrescine can substitute for the lysine residue of the eIF5A precursor. -!- Hypusine is formed from deoxyhypusine by the action of EC 1.14.99.29. -!- Formerly EC 1.1.1.249.
|
UniProtKB Entries (1)
| P49366 |
DHYS_HUMAN
Homo sapiens
Deoxyhypusine synthase
|
PDB Structure
| PDB | 1RQD |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
A New Crystal Structure of Deoxyhypusine Synthase Reveals the Configuration of the Active Enzyme and of an Enzyme-NAD-Inhibitor Ternary Complex
J.Biol.Chem.
|
