CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.60 | 4-Layer Sandwich |
|
3.60.130 | Double-stranded beta-helix |
|
3.60.130.10 | Clavaminate synthase-like |
Domain Context
CATH Clusters
| Superfamily | Clavaminate synthase-like |
| Functional Family | Alpha-ketoglutarate-dependent L-arginine hydroxylase |
Enzyme Information
| 1.14.11.39 |
L-asparagine oxygenase.
based on mapping to UniProt Q9Z4Z5
L-asparagine + 2-oxoglutarate + O(2) = (2S,3S)-3-hydroxyasparagine + succinate + CO(2).
-!- The enzyme is only able to hydroxylate free L-asparagine. -!- It is not active toward D-asparagine. -!- The beta-hydroxylated asparagine produced is incorporated at position 9 of the calcium-dependent antibiotic (CDA), an 11-residue non- ribosomally synthesized acidic lipopeptide lactone. -!- Formerly EC 1.14.11.n1.
|
UniProtKB Entries (1)
| Q9Z4Z5 |
ASNO_STRCO
Streptomyces coelicolor A3(2)
L-asparagine oxygenase
|
PDB Structure
| PDB | 2OG5 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Mechanistic and structural basis of stereospecific Cbeta-hydroxylation in calcium-dependent antibiotic, a daptomycin-type lipopeptide.
Acs Chem.Biol.
|
