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A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.
ENZYME entry: EC 2.6.1.84
| Accepted Name |
|---|
| Arginine--pyruvate transaminase.
|
| Alternative Name(s) |
|---|
| Arginine:pyruvate transaminase. |
| Reaction catalysed |
|---|
| L-arginine + pyruvate <=> 5-guanidino-2-oxopentanoate + L-alanine |
| Cofactor(s) |
|---|
| Pyridoxal 5'-phosphate.
|
| Comment(s) |
|---|
- While L-arginine is the best substrate, the enzyme exhibits broad
substrate specificity, with L-lysine, L-methionine, L-leucine,
L-ornithine and L-glutamine also able to act as substrates, but more
slowly.
- Pyruvate cannot be replaced by 2-oxoglutarate as amino-group
acceptor.
- This is the first catalytic enzyme of the arginine transaminase
pathway for L-arginine utilization in Pseudomonas aeruginosa.
- This pathway is only used when the major route of arginine
catabolism, i.e. the arginine succinyltransferase pathway,
is blocked.
|
| Cross-references |
|---|
| BRENDA | 2.6.1.84 |
| EC2PDB | 2.6.1.84 |
| ExplorEnz | 2.6.1.84 |
| PRIAM enzyme-specific profiles | 2.6.1.84 |
| KEGG Ligand Database for Enzyme Nomenclature | 2.6.1.84 |
| IUBMB Enzyme Nomenclature | 2.6.1.84 |
| IntEnz | 2.6.1.84 |
| MEDLINE | Find literature relating to 2.6.1.84 |
| MetaCyc | 2.6.1.84 |
| UniProtKB/Swiss-Prot |
|
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All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 2.6.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.6.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-