| EC |
2.7.3.3 |
| Accepted name: |
arginine kinase |
| Reaction: |
ATP + L-arginine = ADP + Nω-phospho-L-arginine |
| Other name(s): |
arginine phosphokinase; adenosine 5′-triphosphate: L-arginine phosphotransferase; adenosine 5′-triphosphate-arginine phosphotransferase; ATP:L-arginine N-phosphotransferasel ATP:L-arginine ω-N-phosphotransferase |
| Systematic name: |
ATP:L-arginine Nω-phosphotransferase |
| Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9026-70-4 |
| References: |
| 1. |
Elödi, P. and Szörényi, E.T. Properties of crystalline arginine phosphoferase isolated from crustacean muscle. Acta Physiol. Acad. Sci. (Hung.) 9 (1956) 367–379. [PMID: 13339436] |
| 2. |
Morrison, J.F., Griffiths, D.E. and Ennor, A.H. The purification and properties of arginine phosphokinase. Biochem. J. 65 (1957) 143–153. [PMID: 13403885] |
| 3. |
Szörényi, E.T., Dvornikova, P.D. and Degtyar, P.G. [Isolation in the crystalline state and some properties of adenosinetriphosphate-arginine transphosphorylase.] Dokl. Akad. Nauk SSSR. 67 (1949) 341–344. (in Russian) |
| 4. |
Virden, R., Watts, D.C. and Baldwin, E. Adenosine 5′-triphosphate-arginine phosphotransferase from lobster muscle: purification and properties. Biochem. J. 94 (1965) 536–544. [PMID: 14340045] |
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| [EC 2.7.3.3 created 1961] |
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