Arginine—pyruvate transaminase
| Arginine-pyruvate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.84 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Arginine-pyruvate transaminase (EC 2.6.1.84) is a pyridoxal phosphate-dependent enzyme that catalyzes the chemical reaction
The two substrates of this enzyme characterised from Pseudomonas aeruginosa are L-arginine and pyruvic acid. Its products are 5-guanidino-2-oxopentanoic acid and L-alanine. In this bacterium, the reaction is the first step in a breakdown of the amino acid arginine.[1][2]
This enzyme is a transferase, specifically a transaminase, which transfer nitrogenous groups. The systematic name of this enzyme class is L-arginine:pyruvate aminotransferase. Other names in common use include arginine:pyruvate transaminase, and AruH.[3]
References
- ↑ Yang Z, Lu CD (2007). "Characterization of an arginine:pyruvate transaminase in arginine catabolism of Pseudomonas aeruginosa PAO1". J. Bacteriol. 189 (11): 3954–9. doi:10.1128/JB.00262-07. PMC 1913410. PMID 17416668.
- ↑ Yang Z, Lu CD (2007). "Functional genomics enables identification of genes of the arginine transaminase pathway in Pseudomonas aeruginosa". J. Bacteriol. 189 (11): 3945–53. doi:10.1128/JB.00261-07. PMC 1913404. PMID 17416670.
- ↑ Enzyme 2.6.1.84 at KEGG Pathway Database.
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