ENZYME entry: EC 1.4.99.6
| Accepted Name |
|---|
| D-arginine dehydrogenase.
|
| Alternative Name(s) |
|---|
| D-amino-acid dehydrogenase. |
| Reaction catalysed |
|---|
| D-arginine + acceptor + H(2)O <=> 5-guanidino-2-oxopentanoate + NH(3) + reduced acceptor |
| Cofactor(s) |
|---|
| FAD.
|
| Comment(s) |
|---|
- The enzyme, which has been isolated from the bacterium Pseudomonas
aeruginosa PAO1, forms with EC 1.4.1.25 a two-enzyme complex involved
in the racemization of D- and L-arginine.
- The enzyme has a broad substrate range and can act on most D-amino
acids with the exception of D-glutamate and D-aspartate.
- However, activity is maximal with D-arginine and D-lysine.
- Not active on glycine.
- Formerly EC 1.4.99.1.
|
| Cross-references |
|---|
| BRENDA | 1.4.99.6 |
| EC2PDB | 1.4.99.6 |
| ExplorEnz | 1.4.99.6 |
| PRIAM enzyme-specific profiles | 1.4.99.6 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.4.99.6 |
| IUBMB Enzyme Nomenclature | 1.4.99.6 |
| IntEnz | 1.4.99.6 |
| MEDLINE | Find literature relating to 1.4.99.6 |
| MetaCyc | 1.4.99.6 |
| Rhea expert-curated reactions | 1.4.99.6 |
| UniProtKB/Swiss-Prot |
|
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