Acetat kinaza

Acetat kinaza
Identifikatori
EC broj2.7.2.1
CAS broj9027-42-3
Baze podataka
IntEnzIntEnz pregled
BRENDABRENDA pristup
ExPASyNiceZyme pregled
KEGGKEGG pristup
MetaCycmetabolički put
PRIAMprofil
Strukture PBPRCSB PDB PDBe PDBj PDBsum

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

ATP + acetat ADP + acetil fosfat

Za rad ovog enzima je neophodan jon Mg2+.

Reference

  1. ^ 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. 
  2. ^ Romano, A.H. & Nickerson, W.J. (1954). „Cystine reductase of pea seeds and yeast”. J. Biol. Chem. 208: 409—416. PMID 13174550. 
  3. ^ Stern, J.R. & Ochoa, S. (1951). „Enzymatic synthesis of citric acid. I. Synthesis with soluble enzymes”. J. Biol. Chem. 191: 161—172. PMID 14850456. 
  4. ^ 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. 
  5. ^ 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. 
  6. ^ 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. 
  7. ^ 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. 
  8. ^ 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. 
  9. ^ 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

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