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 |
|
View entry in original ENZYME format
View entry in raw text format (no links)
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 1.4.99.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.4.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-