Arginine kinase

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 / EGO
Search PMC articles PubMed articles NCBI proteins

In enzymology, an arginine kinase (EC 2.7.3.3) is an enzyme that catalyzes the chemical reaction

ATP + L-arginine $\rightleftharpoons$ ADP + N^ω-phospho-L-arginine

Thus, the two substrates of this enzyme are ATP and L-arginine, whereas its two products are ADP and N^ω-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 N^ω-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. 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. PMC 1206586. PMID 14340045.