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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