Arginin kinaza
| Arginin kinaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.7.3.3 | ||||||||
| CAS broj | 9026-70-4 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Arginin kinaza (EC 2.7.3.3, argininska fosfokinaza, adenozinska 5'-trifosfat:L-argininska fosfotransferaza, adenozin 5'-trifosfat-arginin fosfotransferaza, ATP:L-arginin N-fosfotransferazal ATP:L-arginin omega-N-fosfotransferaza) je enzim sa sistematskim imenom ATP:L-arginin Nomega-fosfotransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- ATP + L-arginin ADP + Nomega-fosfo-L-arginin
Reference
- ↑ Elödi, P. and Szörényi, E.T. (1956). „Properties of crystalline arginine phosphoferase isolated from crustacean muscle”. Acta Physiol. Acad. Sci. (Hung.) 9: 367-379. PMID 13339436.
- ↑ Morrison, J.F., Griffiths, D.E. and Ennor, A.H. (1957). „The purification and properties of arginine phosphokinase”. Biochem. J. 65: 143-153. PMID 13403885.
- ↑ Szörényi, E.T., Dvornikova, P.D. and Degtyar, P.G. (1949). „[Isolation in the crystalline state and some properties of adenosinetriphosphate-arginine transphosphorylase.]”. Dokl. Akad. Nauk SSSR. 67: 341-344.
- ↑ Virden, R., Watts, D.C. and Baldwin, E. (1965). „Adenosine 5′-triphosphate-arginine phosphotransferase from lobster muscle: purification and properties”. Biochem. J. 94: 536-544. PMID 14340045.
Literatura
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.
Vanjske veze
- MeSH Arginine+kinase
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
