Acetat kinaza
Acetat kinaza (EC 2.7.2.1, acetokinaza, AckA, AK, sirćetna kinaza, acetatna kinaza (fosforilacija)) je enzim sa sistematskim imenom ATP:acetat fosfotransferaza.[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Acetat kinaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Acetat kinaza homodimer, Methanosarcina thermophila | |||||||||
| Identifikatori | |||||||||
| EC broj | 2.7.2.1 | ||||||||
| CAS broj | 9027-42-3 | ||||||||
| 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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Za rad ovog enzima je neophodan jon Mg2+.
Reference uredi
- ↑ Romain, Y., Demassieux, S. and Carriere, S. (1982). „Partial purification and characterization of two isoenzymes involved in the sulfurylation of catecholamines”. Biochem. Biophys. Res. Commun. 106: 999-1005. PMID 6956338.
- ↑ Romano, A.H. and Nickerson, W.J. (1954). „Cystine reductase of pea seeds and yeast”. J. Biol. Chem. 208: 409-416. PMID 13174550.
- ↑ Stern, J.R. and Ochoa, S. (1951). „Enzymatic synthesis of citric acid. I. Synthesis with soluble enzymes”. J. Biol. Chem. 191: 161-172. PMID 14850456.
- ↑ Fox, D.K. and Roseman, S. (1986). „Isolation and characterization of homogeneous acetate kinase from Salmonella typhimurium and Escherichia coli”. J. Biol. Chem. 261: 13487-13497. PMID 3020034.
- ↑ Knorr, R., Ehrmann, M.A. and Vogel, R.F. (2001). „Cloning, expression, and characterization of acetate kinase from Lactobacillus sanfranciscensis”. Microbiol. Res. 156: 267-277. PMID 11716215.
- ↑ Buss, K.A., Cooper, D.R., Ingram-Smith, C., Ferry, J.G., Sanders, D.A. and Hasson, M.S. (2001). „Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases”. J. Bacteriol. 183: 680-686. PMID 11133963.
- ↑ Ingram-Smith, C., Gorrell, A., Lawrence, S.H., Iyer, P., Smith, K. and Ferry, J.G. (2005). „Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase”. J. Bacteriol. 187: 2386-2394. PMID 15774882.
- ↑ Gorrell, A., Lawrence, S.H. and Ferry, J.G. (2005). „Structural and kinetic analyses of arginine residues in the active site of the acetate kinase from Methanosarcina thermophila”. J. Biol. Chem. 280: 10731-10742. PMID 15647264.
- ↑ Heßlinger, C., Fairhurst, S.A. and Sawers, G. (1998). „Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate”. Mol. Microbiol. 27: 477-492. PMID 9484901.
Literatura uredi
- 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.