Arginine kinase
In enzymology, arginine kinase (EC 2.7.3.3) is an enzyme that catalyzes the chemical reaction
- ATP + L-arginine ADP + Nω-phospho-L-arginine
| arginine kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.7.3.3 | ||||||||
| CAS number | 9026-70-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Thus, the two substrates of this enzyme are ATP and L-arginine, whereas its two products are ADP and Nω-phospho-L-arginine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:L-arginine Nω-phosphotransferase. Other names in common use include arginine phosphokinase, adenosine 5'-triphosphate: L-arginine phosphotransferase, adenosine 5'-triphosphate-arginine phosphotransferase, ATP:L-arginine N-phosphotransferasel ATP:L-arginine, and ω-N-phosphotransferase. This enzyme participates in arginine and proline metabolism.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1BG0, 1M15, 1M80, 1P50, 1P52, 1RL9, 1SD0, and 2J1Q.
References
- ELODI P, SZORENYI E (1956). "Properties of crystalline arginine-phosphoferase isolated from Crustacean muscle". Acta Physiol. Hung. 9 (4): 367–79. PMID 13339436.
- MORRISON JF, GRIFFITHS DE, ENNOR AH (1957). "The purification and properties of arginine phosphokinase". Biochem. J. 65 (1): 143–53. doi:10.1042/bj0650143. PMC 1199841. PMID 13403885.
- Z; Fancsovits, P; Akos, M; Tóthné Gilán, Z; Hauzman, E; Papp, Z (2006). "[In vitro fertilization at our department. A decade's work in figures and facts (1994-2003)]". Orv. Hetil. 147 (1): 7–14. PMID 16519065.
- VIRDEN R, WATTS DC, BALDWIN E (1965). "Adenosine 5′-triphosphate–arginine phosphotransferase from lobster muscle: purification and properties". Biochem. J. 94 (3): 536–44. doi:10.1042/bj0940536. PMC 1206586. PMID 14340045.