Kreatin kinaza
| Kreatin kinaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Kreatin kinaza MM, homodimer, Human | |||||||||
| Identifikatori | |||||||||
| EC broj | 2.7.3.2 | ||||||||
| CAS broj | 9001-15-4 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Kreatin kinaza (EC 2.7.3.2, ATP:kreatin fosfotransferaza, CK, MM-CK, MB-CK, BB-CK, kreatinska fosfokinaza, kreatinska fosfotransferaza, fosfokreatinska kinaza, adenozin trifosfat-kreatinska transfosforilaza, Mi-CK, CK-BB, CK-MM, CK-MB, CKMiMi, MiMi-CK) je enzim sa sistematskim imenom ATP:kreatin N-fosfotransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
- ATP + kreatin ADP + fosfokreatin
N-etilglikocijamin takođe može da deluje kao akceptor.
Reference
- ↑ Ennor, A.H., Rosenberg, H. and Armstrong, M.D. (1955). „Specificity of creatine phosphokinase”. Nature 175: 120-120. PMID 13235819.
- ↑ Keutel, H.J., Jacobs, H.K., Okabe, K., Yue, R.H. and Kuby, S.A. (1968). „Studies on adenosine triphosphate transphosphorylases. VII. Isolation of the crystalline adenosine triphosphate-creatine transphosphorylase from calf brain”. Biochemistry 7: 4283-4290. PMID 5750168.
- ↑ Kuby, S.A., Noda, L. and Lardy, H.A. (1954). „Adenosine triphosphate-creatine transphosphorylase. I. Isolation of the crystalline enzyme from rabbit muscle”. J. Biol. Chem. 209: 191-201. PMID 13192073.
- ↑ Kuby, S.A. and Noltmann, E.A. (1962). „ATP-creatine transphosphorylase”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 6 (2nd izd.). New York: Academic Press. str. 515-603.
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.
- Kuby, S.A. and Noltmann, E.A. (1962). „ATP-creatine transphosphorylase”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 6 (2nd izd.). New York: Academic Press. str. 515-603.
Spoljašnje veze
- MeSH Creatine+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
