Adenilat kinaza
(Preusmjereno sa stranice Myokinase)
| Adenilat kinaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifikatori | |||||||||
| EC broj | 2.7.4.3 | ||||||||
| CAS broj | 2598011 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Adenilat kinaza (EC 2.7.4.3, miokinaza, 5'-AMP-kinaza, adenilna kinaza, adenilokinaza) je enzim sa sistematskim imenom ATP:AMP fosfotransferaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
Neorganski trifosfat takođe može da deluje kao donor.
- ↑ Chiga, M. and Plaut, G.W.E. (1960). „Nucleotide transphosphorylases from liver. I. Purification and properties of an adenosine triphosphate-adenosine monophosphate transphosphorylase from swine liver”. J. Biol. Chem. 235: 3260-3265. PMID 13693070.
- ↑ Saint Girons, I.S., Gilles, A.-M., Margarita, D., Michelson, S., Monnot, M., Fermandjian, S., Danchin, A. and Barzu, O. (1987). „Structural and catalytic characteristics of Escherichia coli adenylate kinase”. J. Biol. Chem. 262: 622-629. PMID 3027060.
- ↑ Noda, L. (1958). „Adenosine triphosphate-adenosine monophosphate transphosphorylase. III. Kinetic studies”. J. Biol. Chem. 232: 237-250. PMID 13549414.
- ↑ Noda, L. (1962). „Nucleoside triphosphate-nucleoside monophosphokinases”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 6 (2nd izd.). New York: Academic Press. str. 139-149.
- ↑ Noda, L. and Kuby, S.A. (1957). „Adenosine triphosphate-adenosine monophosphate transphosphorylase (myokinase). I. Isolation of the crystalline enzyme from rabbit skeletal muscle”. J. Biol. Chem. 226: 541-549. PMID 13428784.
- ↑ Noda, L. and Kuby, S.A. (1957). „Adenosine triphosphate-adenosine monophosphate transphosphorylase (myokinase). II. Homogeneity measurements and physicochemical properties”. J. Biol. Chem. 226: 551-558. PMID 13428785.
- ↑ Oliver, I.T. and Peel, J.L. (1956). „Myokinase activity in microorganisms”. Biochim. Biophys. Acta 20: 390-392. PMID 13328866.
- 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.
- Noda, L. (1962). „Nucleoside triphosphate-nucleoside monophosphokinases”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 6 (2nd izd.). New York: Academic Press. str. 139-149.