Arginine kinase

Jump to: navigation, search

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

ATP + L-arginine ADP + Nomega-phospho-L-arginine

Thus, the two substrates of this enzyme are ATP and L-arginine, whereas its two products are ADP and Nomega-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 Nomega-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 omega-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

  • IUBMB entry for 2.7.3.3
  • BRENDA references for 2.7.3.3 (Recommended.)
  • PubMed references for 2.7.3.3
  • PubMed Central references for 2.7.3.3
  • Google Scholar references for 2.7.3.3
  • ELODI P, SZORENYI E (1956). "Properties of crystalline arginine-phosphoferase isolated from Crustacean muscle". Acta. Physiol. Hung. 9: 367&ndash, 79. PMID 13339436.
  • MORRISON JF, GRIFFITHS DE, ENNOR AH (1957). "The purification and properties of arginine phosphokinase". Biochem. J. 65: 143&ndash, 53. PMID 13403885.
  • Z (2006). "[In vitro fertilization at our department. A decade's work in figures and facts (1994-2003)]". Orv. Hetil. 147: 7&ndash, 14. PMID 16519065.
  • VIRDEN R, WATTS DC, BALDWIN E (1965). "ADENOSINE 5'-TRIPHOSPHATE-ARGININE PHOSPHOTRANSFERASE FROM LOBSTER MUSCLE: PURIFICATION AND PROPERTIES". Biochem. J. 94: 536&ndash, 44. PMID 14340045.

External links

The CAS registry number for this enzyme class is 9026-70-4.

Gene Ontology (GO) codes


Linked-in.jpg