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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| Identifikatori | |||||||||
| EC broj | 2.7.2.1 | ||||||||
| CAS broj | 9027-42-3 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Za rad ovog enzima je neophodan jon Mg2+.
Reference уреди
- ^ 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. & Nickerson, W.J. (1954). „Cystine reductase of pea seeds and yeast”. J. Biol. Chem. 208: 409—416. PMID 13174550.
- ^ Stern, J.R. & Ochoa, S. (1951). „Enzymatic synthesis of citric acid. I. Synthesis with soluble enzymes”. J. Biol. Chem. 191: 161—172. PMID 14850456.
- ^ Fox, D.K. & 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 уреди
- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
- William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.
Spoljašnje veze уреди
- Acetate+kinase на US National Library of Medicine Medical Subject Headings (MeSH)
